https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_14&feed=atom&action=historyCarbohydrate Binding Module Family 14 - Revision history2024-03-28T19:03:20ZRevision history for this page on the wikiMediaWiki 1.35.10https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_14&diff=16679&oldid=prevHarry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"2021-12-18T21:20:05Z<p>Text replacement - "\^\^\^(.*)\^\^\^" to "<a href="/index.php?title=User:$1&action=edit&redlink=1" class="new" title="User:$1 (page does not exist)">$1</a>"</p>
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</table>Harry Brumerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_14&diff=16133&oldid=prevHarry Brumer: fixed CAZy DB link2020-12-02T17:29:05Z<p>fixed CAZy DB link</p>
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</table>Harry Brumerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_14&diff=16131&oldid=prevElizabeth Ficko-Blean at 17:14, 2 December 20202020-12-02T17:14:59Z<p></p>
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<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>{{<del class="diffchange diffchange-inline">UnderConstruction</del>}}</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>{{<ins class="diffchange diffchange-inline">CuratorApproved</ins>}}</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Author]]: ^^^Eva Madland^^^</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Author]]: ^^^Eva Madland^^^</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Responsible Curator]]: ^^^Elizabeth Ficko-Blean^^^</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Responsible Curator]]: ^^^Elizabeth Ficko-Blean^^^</div></td></tr>
</table>Elizabeth Ficko-Bleanhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_14&diff=16130&oldid=prevEva Madland at 13:19, 2 December 20202020-12-02T13:19:41Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Ligand specificities ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Ligand specificities ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Family 14 CBMs are modules composed of approximately 70 residues. These modules have been reported to be associated with chitinases <cite>Fadel2016</cite> and as chitin-binding lectins e.g. effector proteins from the tomato pathogens ''Pseudoercospora fuligena'' or ''Cladosporium fulvum'' <cite>Kohler2016 Hurlburt2018</cite>, as an antimicrobial protein (tachycitin) from horseshoe crab hemocytes <cite>Kawabata1996</cite> and in peritrophic matrix proteins from the malaria vector ''Anopheles gambia'' <cite>Shen1998</cite>. Members of CBM14 have been shown to bind chitin <cite>Shen1998 Vandevenne2011 Madland2019</cite> and chitooligomers <cite>Crasson2016 Hurlburt2018</cite>; binding to 50 % acetylated hyaluronan has also been demonstrated <cite>Crasson2016</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Family 14 CBMs are modules composed of approximately 70 residues. These modules have been reported to be associated with chitinases <cite>Fadel2016</cite> and as chitin-binding lectins e.g. effector proteins from the tomato pathogens ''Pseudoercospora fuligena'' or ''Cladosporium fulvum'' <cite>Kohler2016 Hurlburt2018</cite>, as an antimicrobial protein (tachycitin) from horseshoe crab <ins class="diffchange diffchange-inline">(''Tachypleus tridentatus'') </ins>hemocytes <cite>Kawabata1996</cite> and in peritrophic matrix proteins from the malaria vector ''Anopheles gambia'' <cite>Shen1998</cite>. Members of CBM14 have been shown to bind chitin <cite>Shen1998 Vandevenne2011 Madland2019</cite> and chitooligomers <cite>Crasson2016 Hurlburt2018</cite>; binding to 50 % acetylated hyaluronan has also been demonstrated <cite>Crasson2016</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The ligand binding affinities have been quantified for two CBM14 members. The interaction between a CBM14 from human chitotriosidase-1 (CHIT1, characterized as a glycoside hydrolase family 18 ([[GH18]])) and (GlcNAc)<sub>3</sub> has been investigated. The CBM14 displayed a relatively weak interaction of K<sub>D</sub> 9.9 &plusmn; 0.8 mM using NMR titration experiments <cite>Crasson2016</cite> and K<sub>D</sub> 3.1 &plusmn; 0.2 mM using isothermal titration calorimetry (ITC) <cite>Madland2019</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The ligand binding affinities have been quantified for two CBM14 members. The interaction between a CBM14 from human chitotriosidase-1 (CHIT1, characterized as a glycoside hydrolase family 18 ([[GH18]])) and (GlcNAc)<sub>3</sub> has been investigated. The CBM14 displayed a relatively weak interaction of K<sub>D</sub> 9.9 &plusmn; 0.8 mM using NMR titration experiments <cite>Crasson2016</cite> and K<sub>D</sub> 3.1 &plusmn; 0.2 mM using isothermal titration calorimetry (ITC) <cite>Madland2019</cite>.</div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Although some of the structural features described above differ between the CBM14 lectins and ''Hs''CBM14, the common denominator is the involvement of these modules in immune responses <cite>Burg2006 Joosten1997 Fadel2016</cite>. CHIT1 is produced by macrophages and neutrophils <cite>Hollak1994, Kzhyshkowska2007</cite> and is utilized by the innate immune response to combat chitin-containing pathogens <cite>Gordon-Thomson2009</cite>. A different response is found in the tomato pathogen ''C. fulvum''; here, the effector protein utilizes CBM14's ability to bind chitin in the fungal cell wall enabling protection from hydrolysis by plant-derived chitinases during infection <cite>Joosten1997 Burg2006</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Although some of the structural features described above differ between the CBM14 lectins and ''Hs''CBM14, the common denominator is the involvement of these modules in immune responses <cite>Burg2006 Joosten1997 Fadel2016</cite>. CHIT1 is produced by macrophages and neutrophils <cite>Hollak1994, Kzhyshkowska2007</cite> and is utilized by the innate immune response to combat chitin-containing pathogens <cite>Gordon-Thomson2009</cite>. A different response is found in the tomato pathogen ''C. fulvum''; here, the effector protein utilizes CBM14's ability to bind chitin in the fungal cell wall enabling protection from hydrolysis by plant-derived chitinases during infection <cite>Joosten1997 Burg2006</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>;First Identified: CBM14 was first identified as an antimicrobial protein with chitin-binding ability in the hemocyte of horseshoe crab (''<del class="diffchange diffchange-inline">Tachypleus </del>tridentatus'') and called tachycitin <cite>Kawabata1996</cite>. </div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>;First Identified: CBM14 was first identified as an antimicrobial protein with chitin-binding ability in the hemocyte of horseshoe crab (''<ins class="diffchange diffchange-inline">T. </ins>tridentatus'') and called tachycitin <cite>Kawabata1996</cite>. </div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First Structural Characterization: The first three-dimensional structure was determined by NMR spectroscopy for the CBM14 module tachycitin (PDB ID: [{{PDBlink}}1DQC 1DQC]) <cite>Suetake2000</cite>. The structure of the first carbohydrate-active enzyme associated CBM14 was determined by X-ray crystallography for the CBM14 of human chitotriosidase (PDB ID: [{{PDBlink}}5HBF 5HBF]) <cite>Fadel2016</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First Structural Characterization: The first three-dimensional structure was determined by NMR spectroscopy for the CBM14 module tachycitin (PDB ID: [{{PDBlink}}1DQC 1DQC]) <cite>Suetake2000</cite>. The structure of the first carbohydrate-active enzyme associated CBM14 was determined by X-ray crystallography for the CBM14 of human chitotriosidase (PDB ID: [{{PDBlink}}5HBF 5HBF]) <cite>Fadel2016</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
</table>Eva Madlandhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_14&diff=16129&oldid=prevEva Madland at 12:24, 2 December 20202020-12-02T12:24:29Z<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
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<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 12:24, 2 December 2020</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l18" >Line 18:</td>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Ligand specificities ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Ligand specificities ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Family 14 CBMs are modules composed of approximately 70 residues. These modules have been reported to be associated with chitinases <cite>Fadel2016</cite> and as chitin-binding lectins <del class="diffchange diffchange-inline">or lectin-like proteins </del>e.g. effector proteins from the tomato pathogens ''Pseudoercospora fuligena'' or ''Cladosporium fulvum'' <cite>Kohler2016 Hurlburt2018</cite>, as an antimicrobial <del class="diffchange diffchange-inline">lectin-like </del>protein (tachycitin) from horseshoe crab hemocytes <cite>Kawabata1996</cite> and in peritrophic matrix proteins from the malaria vector ''Anopheles gambia'' <cite>Shen1998</cite>. Members of CBM14 have been shown to bind chitin <cite>Shen1998 Vandevenne2011 Madland2019</cite> and chitooligomers <cite>Crasson2016 Hurlburt2018</cite>; binding to 50 % acetylated hyaluronan has also been demonstrated <cite>Crasson2016</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Family 14 CBMs are modules composed of approximately 70 residues. These modules have been reported to be associated with chitinases <cite>Fadel2016</cite> and as chitin-binding lectins e.g. effector proteins from the tomato pathogens ''Pseudoercospora fuligena'' or ''Cladosporium fulvum'' <cite>Kohler2016 Hurlburt2018</cite>, as an antimicrobial protein (tachycitin) from horseshoe crab hemocytes <cite>Kawabata1996</cite> and in peritrophic matrix proteins from the malaria vector ''Anopheles gambia'' <cite>Shen1998</cite>. Members of CBM14 have been shown to bind chitin <cite>Shen1998 Vandevenne2011 Madland2019</cite> and chitooligomers <cite>Crasson2016 Hurlburt2018</cite>; binding to 50 % acetylated hyaluronan has also been demonstrated <cite>Crasson2016</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The ligand binding affinities have been quantified for two CBM14 members. The interaction between a CBM14 from human chitotriosidase-1 (CHIT1, characterized as a glycoside hydrolase family 18 ([[GH18]])) and (GlcNAc)<sub>3</sub> has been investigated. The CBM14 displayed a relatively weak interaction of K<sub>D</sub> 9.9 &plusmn; 0.8 mM using NMR titration experiments <cite>Crasson2016</cite> and K<sub>D</sub> 3.1 &plusmn; 0.2 mM using isothermal titration calorimetry (ITC) <cite>Madland2019</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The ligand binding affinities have been quantified for two CBM14 members. The interaction between a CBM14 from human chitotriosidase-1 (CHIT1, characterized as a glycoside hydrolase family 18 ([[GH18]])) and (GlcNAc)<sub>3</sub> has been investigated. The CBM14 displayed a relatively weak interaction of K<sub>D</sub> 9.9 &plusmn; 0.8 mM using NMR titration experiments <cite>Crasson2016</cite> and K<sub>D</sub> 3.1 &plusmn; 0.2 mM using isothermal titration calorimetry (ITC) <cite>Madland2019</cite>.</div></td></tr>
<tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l36" >Line 36:</td>
<td colspan="2" class="diff-lineno">Line 36:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Although some of the structural features described above differ between the CBM14 lectins and ''Hs''CBM14, the common denominator is the involvement of these modules in immune responses <cite>Burg2006 Joosten1997 Fadel2016</cite>. CHIT1 is produced by macrophages and neutrophils <cite>Hollak1994, Kzhyshkowska2007</cite> and is utilized by the innate immune response to combat chitin-containing pathogens <cite>Gordon-Thomson2009</cite>. A different response is found in the tomato pathogen ''C. fulvum''; here, the effector protein utilizes CBM14's ability to bind chitin in the fungal cell wall enabling protection from hydrolysis by plant-derived chitinases during infection <cite>Joosten1997 Burg2006</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Although some of the structural features described above differ between the CBM14 lectins and ''Hs''CBM14, the common denominator is the involvement of these modules in immune responses <cite>Burg2006 Joosten1997 Fadel2016</cite>. CHIT1 is produced by macrophages and neutrophils <cite>Hollak1994, Kzhyshkowska2007</cite> and is utilized by the innate immune response to combat chitin-containing pathogens <cite>Gordon-Thomson2009</cite>. A different response is found in the tomato pathogen ''C. fulvum''; here, the effector protein utilizes CBM14's ability to bind chitin in the fungal cell wall enabling protection from hydrolysis by plant-derived chitinases during infection <cite>Joosten1997 Burg2006</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>;First Identified: CBM14 was first identified as an antimicrobial <del class="diffchange diffchange-inline">lectin-like </del>protein with chitin-binding ability in the hemocyte of horseshoe crab (''Tachypleus tridentatus'') and called tachycitin <cite>Kawabata1996</cite>. </div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>;First Identified: CBM14 was first identified as an antimicrobial protein with chitin-binding ability in the hemocyte of horseshoe crab (''Tachypleus tridentatus'') and called tachycitin <cite>Kawabata1996</cite>. </div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First Structural Characterization: The first three-dimensional structure was determined by NMR spectroscopy for the CBM14 module tachycitin (PDB ID: [{{PDBlink}}1DQC 1DQC]) <cite>Suetake2000</cite>. The structure of the first carbohydrate-active enzyme associated CBM14 was determined by X-ray crystallography for the CBM14 of human chitotriosidase (PDB ID: [{{PDBlink}}5HBF 5HBF]) <cite>Fadel2016</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First Structural Characterization: The first three-dimensional structure was determined by NMR spectroscopy for the CBM14 module tachycitin (PDB ID: [{{PDBlink}}1DQC 1DQC]) <cite>Suetake2000</cite>. The structure of the first carbohydrate-active enzyme associated CBM14 was determined by X-ray crystallography for the CBM14 of human chitotriosidase (PDB ID: [{{PDBlink}}5HBF 5HBF]) <cite>Fadel2016</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
</table>Eva Madlandhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_14&diff=16128&oldid=prevEva Madland at 10:53, 2 December 20202020-12-02T10:53:32Z<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
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<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 10:53, 2 December 2020</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l34" >Line 34:</td>
<td colspan="2" class="diff-lineno">Line 34:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Several members of CBM14 are often encountered as chitin-binding lectins <cite>Kawabata1996 Burg2004 Suetake2000 Kohler2016 Hurlburt2018</cite>, while the members present in modular chitinases play a key role in targeting substrate <cite>Renkema1997 Tjoelker2000 Fadel2016</cite>. The most common associated modules are chitinases, e.g. [[GH18]] from human chitotriosidase structurally determined together with ''Hs''CBM14 (PDB ID: [{{PDBlink}}5HBF 5HBF])<cite>Fadel2016</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Several members of CBM14 are often encountered as chitin-binding lectins <cite>Kawabata1996 Burg2004 Suetake2000 Kohler2016 Hurlburt2018</cite>, while the members present in modular chitinases play a key role in targeting substrate <cite>Renkema1997 Tjoelker2000 Fadel2016</cite>. The most common associated modules are chitinases, e.g. [[GH18]] from human chitotriosidase structurally determined together with ''Hs''CBM14 (PDB ID: [{{PDBlink}}5HBF 5HBF])<cite>Fadel2016</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Although some of the structural features described above differ between the CBM14 lectins and ''Hs''CBM14, the common denominator is the involvement of these modules in immune responses. CHIT1 is produced by macrophages and neutrophils <cite>Hollak1994, Kzhyshkowska2007</cite> and is utilized by the innate immune response to combat chitin-containing pathogens <cite>Gordon-Thomson2009</cite>. A different response is found in the tomato pathogen ''C. fulvum''; here, the effector protein utilizes CBM14's ability to bind chitin in the fungal cell wall enabling protection from hydrolysis by plant-derived chitinases during infection <cite>Joosten1997 Burg2006</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Although some of the structural features described above differ between the CBM14 lectins and ''Hs''CBM14, the common denominator is the involvement of these modules in immune responses <ins class="diffchange diffchange-inline"><cite>Burg2006 Joosten1997 Fadel2016</cite></ins>. CHIT1 is produced by macrophages and neutrophils <cite>Hollak1994, Kzhyshkowska2007</cite> and is utilized by the innate immune response to combat chitin-containing pathogens <cite>Gordon-Thomson2009</cite>. A different response is found in the tomato pathogen ''C. fulvum''; here, the effector protein utilizes CBM14's ability to bind chitin in the fungal cell wall enabling protection from hydrolysis by plant-derived chitinases during infection <cite>Joosten1997 Burg2006</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First Identified: CBM14 was first identified as an antimicrobial lectin-like protein with chitin-binding ability in the hemocyte of horseshoe crab (''Tachypleus tridentatus'') and called tachycitin <cite>Kawabata1996</cite>. </div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First Identified: CBM14 was first identified as an antimicrobial lectin-like protein with chitin-binding ability in the hemocyte of horseshoe crab (''Tachypleus tridentatus'') and called tachycitin <cite>Kawabata1996</cite>. </div></td></tr>
</table>Eva Madlandhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_14&diff=16127&oldid=prevEva Madland at 10:52, 2 December 20202020-12-02T10:52:36Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 10:52, 2 December 2020</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l32" >Line 32:</td>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>CBM14 from the tomato pathogen ''C. fulvum'' (''Cf''CBM14) was the first of these modules to be co-crystallized with (GlcNAc)<sub>6</sub> (PDB ID: [{{PDBlink}}6BN0 6BN0])<cite>Hurlburt2018</cite>. Although the fold of ''Cf''CBM14 is the same as ''Hs''CBM14 (PDB ID: [{{PDBlink}}5HBF 5HBF] and [{{PDBlink}}6SO0 6SO0]) and other [http://www.cazy.org/CBM14_structure.html structurally characterized CBM14 members], the residues responsible for binding differ. Binding of (GlcNAc)<sub>6</sub> is mediated by Lys49, Cys50, Met51, Pro53, Lys99, Trp100, Cys101, Asp102 and Tyr103 positioned along a shallow trench in the longitudinal axis of ''Cf''CBM14 (Figure 1C and D). Mutational studies showed that binding to (GlcNAc)<sub>6</sub> was abolished by mutation of Trp100 and Asp102. The main interaction is reported to be a CH-&pi; stacking between Trp100 and GlcNAc-5 aided by Met51 and Pro53 which are both in van der Waal distances to GlcNAc-1 and GlcNAc-3, respectively <cite>Hurlburt2018</cite>. Although equivalents to Trp100, Asp102 and Tyr103 have been reported to be important for chitin-binding in CBM14 from tomato pathogen ''P. fuligena'' (''Pf''CBM14) (equivalent residues: Trp94, Asp96 and Tyr97) <cite>Kohler2016</cite>, the extensive hydrogen bond network could point to a different binding mechanism for ''Cf''CBM14 that is more reminiscent of a [[Carbohydrate-binding_modules#Types|type B]] CBM.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>CBM14 from the tomato pathogen ''C. fulvum'' (''Cf''CBM14) was the first of these modules to be co-crystallized with (GlcNAc)<sub>6</sub> (PDB ID: [{{PDBlink}}6BN0 6BN0])<cite>Hurlburt2018</cite>. Although the fold of ''Cf''CBM14 is the same as ''Hs''CBM14 (PDB ID: [{{PDBlink}}5HBF 5HBF] and [{{PDBlink}}6SO0 6SO0]) and other [http://www.cazy.org/CBM14_structure.html structurally characterized CBM14 members], the residues responsible for binding differ. Binding of (GlcNAc)<sub>6</sub> is mediated by Lys49, Cys50, Met51, Pro53, Lys99, Trp100, Cys101, Asp102 and Tyr103 positioned along a shallow trench in the longitudinal axis of ''Cf''CBM14 (Figure 1C and D). Mutational studies showed that binding to (GlcNAc)<sub>6</sub> was abolished by mutation of Trp100 and Asp102. The main interaction is reported to be a CH-&pi; stacking between Trp100 and GlcNAc-5 aided by Met51 and Pro53 which are both in van der Waal distances to GlcNAc-1 and GlcNAc-3, respectively <cite>Hurlburt2018</cite>. Although equivalents to Trp100, Asp102 and Tyr103 have been reported to be important for chitin-binding in CBM14 from tomato pathogen ''P. fuligena'' (''Pf''CBM14) (equivalent residues: Trp94, Asp96 and Tyr97) <cite>Kohler2016</cite>, the extensive hydrogen bond network could point to a different binding mechanism for ''Cf''CBM14 that is more reminiscent of a [[Carbohydrate-binding_modules#Types|type B]] CBM.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Functionalities == </div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Functionalities == </div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Several members of CBM14 are often encountered as chitin-binding lectins <cite>Kawabata1996 Burg2004 Suetake2000 Kohler2016 Hurlburt2018</cite>, while the members present in modular chitinases play a key role in targeting substrate. The most common associated modules are chitinases, e.g. [[GH18]] from human chitotriosidase structurally determined together with ''Hs''CBM14 (PDB ID: [{{PDBlink}}5HBF 5HBF])<cite>Fadel2016</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Several members of CBM14 are often encountered as chitin-binding lectins <cite>Kawabata1996 Burg2004 Suetake2000 Kohler2016 Hurlburt2018</cite>, while the members present in modular chitinases play a key role in targeting substrate <ins class="diffchange diffchange-inline"><cite>Renkema1997 Tjoelker2000 Fadel2016</cite></ins>. The most common associated modules are chitinases, e.g. [[GH18]] from human chitotriosidase structurally determined together with ''Hs''CBM14 (PDB ID: [{{PDBlink}}5HBF 5HBF])<cite>Fadel2016</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Although some of the structural features described above differ between the CBM14 lectins and ''Hs''CBM14, the common denominator is the involvement of these modules in immune responses. CHIT1 is produced by macrophages and neutrophils <cite>Hollak1994, Kzhyshkowska2007</cite> and is utilized by the innate immune response to combat chitin-containing pathogens <cite>Gordon-Thomson2009</cite>. A <del class="diffchange diffchange-inline">similar </del>response is found in the tomato pathogen ''C. fulvum''; here, the effector protein utilizes CBM14's ability to bind chitin in the fungal cell wall enabling protection from hydrolysis by plant-derived chitinases during infection <cite>Joosten1997 Burg2006</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Although some of the structural features described above differ between the CBM14 lectins and ''Hs''CBM14, the common denominator is the involvement of these modules in immune responses. CHIT1 is produced by macrophages and neutrophils <cite>Hollak1994, Kzhyshkowska2007</cite> and is utilized by the innate immune response to combat chitin-containing pathogens <cite>Gordon-Thomson2009</cite>. A <ins class="diffchange diffchange-inline">different </ins>response is found in the tomato pathogen ''C. fulvum''; here, the effector protein utilizes CBM14's ability to bind chitin in the fungal cell wall enabling protection from hydrolysis by plant-derived chitinases during infection <cite>Joosten1997 Burg2006</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First Identified: CBM14 was first identified as an antimicrobial lectin-like protein with chitin-binding ability in the hemocyte of horseshoe crab (''Tachypleus tridentatus'') and called tachycitin <cite>Kawabata1996</cite>. </div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First Identified: CBM14 was first identified as an antimicrobial lectin-like protein with chitin-binding ability in the hemocyte of horseshoe crab (''Tachypleus tridentatus'') and called tachycitin <cite>Kawabata1996</cite>. </div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>#Boraston2004 pmid=15214846</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>#Boraston2004 pmid=15214846</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>#Burg2004 pmid=14769793</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>#Burg2004 pmid=14769793</div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;"></ins></div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">#Renkema1997 pmid=9118991</ins></div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;"></ins></div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">#Tjoelker2000 pmid=10617646</ins></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>#Hollak1994 pmid=8132768</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>#Hollak1994 pmid=8132768</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>#Kzhyshkowska2007 pmid=19662198</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>#Kzhyshkowska2007 pmid=19662198</div></td></tr>
</table>Eva Madlandhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_14&diff=16126&oldid=prevEva Madland at 10:44, 2 December 20202020-12-02T10:44:59Z<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 10:44, 2 December 2020</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l25" >Line 25:</td>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Structural Features ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Structural Features ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[[File:Fig1-cbm14.png|thumb|300px|right|'''Figure 1 Example of CBM14 structures.''' A) CBM14<del class="diffchange diffchange-inline"><sub>CHIT1</sub> </del>(PDB ID: [{{PDBlink}}6SO0 6SO0]) cartoon representation. Residues involved in binding (Trp465 and Asn466) are highlighted in cyan, Leu454 in purple, the two aromatic residues (Phe437 and Phe456) forming a hydrophobic core in white and disulfide briges in orange. B) Surface representation of CBM14<del class="diffchange diffchange-inline"><sub>CHIT1</sub></del>. C) ''Cf''CBM14 (PDB ID: [{{PDBlink}}6BN0 6BN0]) cartoon representation. Residues involved in binding (Lys49, Cys50, Met51, Pro53, Lys99, Trp100, Cys101, Asp102 and Tyr103) are highlighted in cyan, the two aromatic residues (Tyr76 and Trp92) forming the hydrophobic core in white, disulfide briges in orange and (GlcNAc)<sub>6</sub> in blue. D) Surface representation of ''Cf''CBM14.]]</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>[[File:Fig1-cbm14.png|thumb|300px|right|'''Figure 1 Example of CBM14 structures.''' A) <ins class="diffchange diffchange-inline">''Hs''</ins>CBM14 (PDB ID: [{{PDBlink}}6SO0 6SO0]) cartoon representation. Residues involved in binding (Trp465 and Asn466) are highlighted in cyan, Leu454 in purple, the two aromatic residues (Phe437 and Phe456) forming a hydrophobic core in white and disulfide briges in orange. B) Surface representation of <ins class="diffchange diffchange-inline">''Hs''</ins>CBM14. C) ''Cf''CBM14 (PDB ID: [{{PDBlink}}6BN0 6BN0]) cartoon representation. Residues involved in binding (Lys49, Cys50, Met51, Pro53, Lys99, Trp100, Cys101, Asp102 and Tyr103) are highlighted in cyan, the two aromatic residues (Tyr76 and Trp92) forming the hydrophobic core in white, disulfide briges in orange and (GlcNAc)<sub>6</sub> in blue. D) Surface representation of ''Cf''CBM14.]]</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>CBM14 members have a hevein-like fold made up by a central &beta;-sheet (three anti-parallel &beta;-strands) linked to a small &beta;-sheet (two anti-parallel &beta;-strands) by two aromatic residues. The CBM14 members from tomato pathogens also have an N-terminal &alpha;-helix and an extended loop connecting -strands 2 and 3, as well as a C-terminal helical turn <cite>Kohler2016 Hurlburt2018</cite>. The latter is also present in tachycitin <cite>Suetake2000</cite>. In addtion, the CBM14 structures have been reported to contain 3-4 disulfide bridges which also serve as a stabilizing effect on this unique fold <cite>Suetake2000 Fadel2016 Hurlburt2018</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>CBM14 members have a hevein-like fold made up by a central &beta;-sheet (three anti-parallel &beta;-strands) linked to a small &beta;-sheet (two anti-parallel &beta;-strands) by two aromatic residues. The CBM14 members from tomato pathogens also have an N-terminal &alpha;-helix and an extended loop connecting -strands 2 and 3, as well as a C-terminal helical turn <cite>Kohler2016 Hurlburt2018</cite>. The latter is also present in tachycitin <cite>Suetake2000</cite>. In addtion, the CBM14 structures have been reported to contain 3-4 disulfide bridges which also serve as a stabilizing effect on this unique fold <cite>Suetake2000 Fadel2016 Hurlburt2018</cite>.</div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>#Boraston2004 pmid=15214846</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>#Boraston2004 pmid=15214846</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;"></del></div></td><td colspan="2"> </td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>#Burg2004 pmid=14769793</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>#Burg2004 pmid=14769793</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>#Hollak1994 pmid=8132768</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>#Hollak1994 pmid=8132768</div></td></tr>
</table>Eva Madlandhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_14&diff=16125&oldid=prevEva Madland at 10:42, 2 December 20202020-12-02T10:42:03Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Ligand specificities ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Ligand specificities ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Family 14 CBMs are modules composed of approximately 70 residues. These modules have been reported to be associated with chitinases <cite>Fadel2016</cite> and as chitin-binding lectins e.g. effector proteins from the tomato pathogens ''Pseudoercospora fuligena'' or ''Cladosporium fulvum'' <cite>Kohler2016 Hurlburt2018</cite>, as an antimicrobial lectin-like protein (tachycitin) from horseshoe crab hemocytes <cite>Kawabata1996</cite> and in peritrophic matrix proteins from the malaria vector ''Anopheles gambia'' <cite>Shen1998</cite>. Members of CBM14 have been shown to bind chitin <cite>Shen1998 Vandevenne2011 Madland2019</cite> and chitooligomers <cite>Crasson2016 Hurlburt2018</cite>; binding to 50 % acetylated hyaluronan has also been demonstrated <cite>Crasson2016</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Family 14 CBMs are modules composed of approximately 70 residues. These modules have been reported to be associated with chitinases <cite>Fadel2016</cite> and as chitin-binding lectins <ins class="diffchange diffchange-inline">or lectin-like proteins </ins>e.g. effector proteins from the tomato pathogens ''Pseudoercospora fuligena'' or ''Cladosporium fulvum'' <cite>Kohler2016 Hurlburt2018</cite>, as an antimicrobial lectin-like protein (tachycitin) from horseshoe crab hemocytes <cite>Kawabata1996</cite> and in peritrophic matrix proteins from the malaria vector ''Anopheles gambia'' <cite>Shen1998</cite>. Members of CBM14 have been shown to bind chitin <cite>Shen1998 Vandevenne2011 Madland2019</cite> and chitooligomers <cite>Crasson2016 Hurlburt2018</cite>; binding to 50 % acetylated hyaluronan has also been demonstrated <cite>Crasson2016</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The ligand binding affinities have been quantified for two CBM14 members. The interaction between a CBM14 from human chitotriosidase-1 (CHIT1, characterized as a glycoside hydrolase family 18 ([[GH18]])) and (GlcNAc)<sub>3</sub> has been investigated. The CBM14 displayed a relatively weak interaction of K<sub>D</sub> 9.9 &plusmn; 0.8 mM using NMR titration experiments <cite>Crasson2016</cite> and K<sub>D</sub> 3.1 &plusmn; 0.2 mM using isothermal titration calorimetry (ITC) <cite>Madland2019</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The ligand binding affinities have been quantified for two CBM14 members. The interaction between a CBM14 from human chitotriosidase-1 (CHIT1, characterized as a glycoside hydrolase family 18 ([[GH18]])) and (GlcNAc)<sub>3</sub> has been investigated. The CBM14 displayed a relatively weak interaction of K<sub>D</sub> 9.9 &plusmn; 0.8 mM using NMR titration experiments <cite>Crasson2016</cite> and K<sub>D</sub> 3.1 &plusmn; 0.2 mM using isothermal titration calorimetry (ITC) <cite>Madland2019</cite>.</div></td></tr>
<tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l28" >Line 28:</td>
<td colspan="2" class="diff-lineno">Line 28:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>CBM14 members have a hevein-like fold made up by a central &beta;-sheet (three anti-parallel &beta;-strands) linked to a small &beta;-sheet (two anti-parallel &beta;-strands) by two aromatic residues. The CBM14 members from tomato pathogens also have an N-terminal &alpha;-helix and an extended loop connecting -strands 2 and 3, as well as a C-terminal helical turn <cite>Kohler2016 Hurlburt2018</cite>. The latter is also present in tachycitin <cite>Suetake2000</cite>. In addtion, the CBM14 structures have been reported to contain 3-4 disulfide bridges which also serve as a stabilizing effect on this unique fold <cite>Suetake2000 Fadel2016 Hurlburt2018</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>CBM14 members have a hevein-like fold made up by a central &beta;-sheet (three anti-parallel &beta;-strands) linked to a small &beta;-sheet (two anti-parallel &beta;-strands) by two aromatic residues. The CBM14 members from tomato pathogens also have an N-terminal &alpha;-helix and an extended loop connecting -strands 2 and 3, as well as a C-terminal helical turn <cite>Kohler2016 Hurlburt2018</cite>. The latter is also present in tachycitin <cite>Suetake2000</cite>. In addtion, the CBM14 structures have been reported to contain 3-4 disulfide bridges which also serve as a stabilizing effect on this unique fold <cite>Suetake2000 Fadel2016 Hurlburt2018</cite>.</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>With the hevein-like fold and lectin-like properties, members of the CBM14 family are characterized as [[Carbohydrate-binding_modules#Types|type C]] CBMs <cite>Boraston2004</cite>. This is in line with the ligand-binding feature seen for the CBM14 associated with CHIT1 (CBM14<del class="diffchange diffchange-inline"><sub>CHIT1</sub></del>). The binding site is composed of a tryptophan and an asparagine (Trp465 and Asn466) at the C-terminus of the module <cite>Crasson2016</cite> (Figure 1A). These residues create a platform-like binding surface (Figure 1B) commonly seen in [[Carbohydrate-binding_modules#Types|type A]] CBMs and could be the reason for why CBM14<del class="diffchange diffchange-inline"><sub>CHIT1</sub> </del>is also able to bind crystalline chitin. In addition to Trp465 and Asn466, a leucine (Leu454) has been reported to be indirectly involved in binding as it contributes to maintaining a correct orientation for Trp465 <cite>Madland2019</cite>. Binding between CBM14<del class="diffchange diffchange-inline"><sub>CHIT1</sub> </del>and chitotriose is likely to occur through CH-&pi; stacking between the side-chain of Trp465 and the middle pyranose ring and hydrogen bonds between the side-chain of Asn466 and the hydrophilic non-reducing end <cite>Madland2019</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>With the hevein-like fold and lectin-like properties, members of the CBM14 family are characterized as [[Carbohydrate-binding_modules#Types|type C]] CBMs <cite>Boraston2004</cite>. This is in line with the ligand-binding feature seen for the CBM14 associated with CHIT1 (<ins class="diffchange diffchange-inline">''Homo sapiens'' CBM14, ''Hs''</ins>CBM14). The binding site is composed of a tryptophan and an asparagine (Trp465 and Asn466) at the C-terminus of the module <cite>Crasson2016</cite> (Figure 1A). These residues create a platform-like binding surface (Figure 1B) commonly seen in [[Carbohydrate-binding_modules#Types|type A]] CBMs and could be the reason for why <ins class="diffchange diffchange-inline">''Hs''</ins>CBM14 is also able to bind crystalline chitin. In addition to Trp465 and Asn466, a leucine (Leu454) has been reported to be indirectly involved in binding as it contributes to maintaining a correct orientation for Trp465 <cite>Madland2019</cite>. Binding between <ins class="diffchange diffchange-inline">''Hs''</ins>CBM14 and chitotriose is likely to occur through CH-&pi; stacking between the side-chain of Trp465 and the middle pyranose ring and hydrogen bonds between the side-chain of Asn466 and the hydrophilic non-reducing end <cite>Madland2019</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>CBM14 from the tomato pathogen ''C. fulvum'' (''Cf''CBM14) was the first of these modules to be co-crystallized with (GlcNAc)<sub>6</sub> (PDB ID: [{{PDBlink}}6BN0 6BN0])<cite>Hurlburt2018</cite>. Although the fold of ''Cf''CBM14 is the same as CBM14<del class="diffchange diffchange-inline"><sub>CHIT1</sub> </del>(PDB ID: [{{PDBlink}}5HBF 5HBF] and [{{PDBlink}}6SO0 6SO0]) and other [http://www.cazy.org/CBM14_structure.html structurally characterized CBM14 members], the residues responsible for binding differ. Binding of (GlcNAc)<sub>6</sub> is mediated by Lys49, Cys50, Met51, Pro53, Lys99, Trp100, Cys101, Asp102 and Tyr103 positioned along a shallow trench in the longitudinal axis of ''Cf''CBM14 (Figure 1C and D). Mutational studies showed that binding to (GlcNAc)<sub>6</sub> was abolished by mutation of Trp100 and Asp102. The main interaction is reported to be a CH-&pi; stacking between Trp100 and GlcNAc-5 aided by Met51 and Pro53 which are both in van der Waal distances to GlcNAc-1 and GlcNAc-3, respectively <cite>Hurlburt2018</cite>. Although equivalents to Trp100, Asp102 and Tyr103 have been reported to be important for chitin-binding in CBM14 from tomato pathogen ''P. fuligena'' (''Pf''CBM14) (equivalent residues: Trp94, Asp96 and Tyr97) <cite>Kohler2016</cite>, the extensive hydrogen bond network could point to a different binding mechanism for ''Cf''CBM14 that is more reminiscent of a [[Carbohydrate-binding_modules#Types|type B]] CBM.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>CBM14 from the tomato pathogen ''C. fulvum'' (''Cf''CBM14) was the first of these modules to be co-crystallized with (GlcNAc)<sub>6</sub> (PDB ID: [{{PDBlink}}6BN0 6BN0])<cite>Hurlburt2018</cite>. Although the fold of ''Cf''CBM14 is the same as <ins class="diffchange diffchange-inline">''Hs''</ins>CBM14 (PDB ID: [{{PDBlink}}5HBF 5HBF] and [{{PDBlink}}6SO0 6SO0]) and other [http://www.cazy.org/CBM14_structure.html structurally characterized CBM14 members], the residues responsible for binding differ. Binding of (GlcNAc)<sub>6</sub> is mediated by Lys49, Cys50, Met51, Pro53, Lys99, Trp100, Cys101, Asp102 and Tyr103 positioned along a shallow trench in the longitudinal axis of ''Cf''CBM14 (Figure 1C and D). Mutational studies showed that binding to (GlcNAc)<sub>6</sub> was abolished by mutation of Trp100 and Asp102. The main interaction is reported to be a CH-&pi; stacking between Trp100 and GlcNAc-5 aided by Met51 and Pro53 which are both in van der Waal distances to GlcNAc-1 and GlcNAc-3, respectively <cite>Hurlburt2018</cite>. Although equivalents to Trp100, Asp102 and Tyr103 have been reported to be important for chitin-binding in CBM14 from tomato pathogen ''P. fuligena'' (''Pf''CBM14) (equivalent residues: Trp94, Asp96 and Tyr97) <cite>Kohler2016</cite>, the extensive hydrogen bond network could point to a different binding mechanism for ''Cf''CBM14 that is more reminiscent of a [[Carbohydrate-binding_modules#Types|type B]] CBM.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Functionalities == </div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Functionalities == </div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Several members of CBM14 are often encountered as chitin-binding lectins <cite>Kawabata1996 Burg2004 Suetake2000 Kohler2016 Hurlburt2018</cite>, while the members present in modular chitinases play a key role in targeting substrate. The most common associated modules are chitinases, e.g. [[GH18]] from human chitotriosidase structurally determined together with CBM14<del class="diffchange diffchange-inline"><sub>CHIT1</sub> </del>(PDB ID: [{{PDBlink}}5HBF 5HBF])<cite>Fadel2016</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Several members of CBM14 are often encountered as chitin-binding lectins <cite>Kawabata1996 Burg2004 Suetake2000 Kohler2016 Hurlburt2018</cite>, while the members present in modular chitinases play a key role in targeting substrate. The most common associated modules are chitinases, e.g. [[GH18]] from human chitotriosidase structurally determined together with <ins class="diffchange diffchange-inline">''Hs''</ins>CBM14 (PDB ID: [{{PDBlink}}5HBF 5HBF])<cite>Fadel2016</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Although some of the structural features described above differ between the CBM14 lectins and CBM14<del class="diffchange diffchange-inline"><sub>CHIT1</sub></del>, the common denominator is the involvement of these modules in immune responses. CHIT1 is produced by macrophages and neutrophils <cite>Hollak1994, Kzhyshkowska2007</cite> and is utilized by the innate immune response to combat chitin-containing pathogens <cite>Gordon-Thomson2009</cite>. A similar response is found in the tomato pathogen ''C. fulvum''; here, the effector protein utilizes CBM14's ability to bind chitin in the fungal cell wall enabling protection from hydrolysis by plant-derived chitinases during infection <cite>Joosten1997 Burg2006</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Although some of the structural features described above differ between the CBM14 lectins and <ins class="diffchange diffchange-inline">''Hs''</ins>CBM14, the common denominator is the involvement of these modules in immune responses. CHIT1 is produced by macrophages and neutrophils <cite>Hollak1994, Kzhyshkowska2007</cite> and is utilized by the innate immune response to combat chitin-containing pathogens <cite>Gordon-Thomson2009</cite>. A similar response is found in the tomato pathogen ''C. fulvum''; here, the effector protein utilizes CBM14's ability to bind chitin in the fungal cell wall enabling protection from hydrolysis by plant-derived chitinases during infection <cite>Joosten1997 Burg2006</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First Identified: CBM14 was first identified as an antimicrobial lectin-like protein with chitin-binding ability in the hemocyte of horseshoe crab (''Tachypleus tridentatus'') and called tachycitin <cite>Kawabata1996</cite>. </div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First Identified: CBM14 was first identified as an antimicrobial lectin-like protein with chitin-binding ability in the hemocyte of horseshoe crab (''Tachypleus tridentatus'') and called tachycitin <cite>Kawabata1996</cite>. </div></td></tr>
</table>Eva Madlandhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_14&diff=16097&oldid=prevElizabeth Ficko-Blean at 19:09, 30 November 20202020-11-30T19:09:07Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 19:09, 30 November 2020</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l36" >Line 36:</td>
<td colspan="2" class="diff-lineno">Line 36:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Although some of the structural features described above differ between the CBM14 lectins and CBM14<sub>CHIT1</sub>, the common denominator is the involvement of these modules in immune responses. CHIT1 is produced by macrophages and neutrophils <cite>Hollak1994, Kzhyshkowska2007</cite> and is utilized by the innate immune response to combat chitin-containing pathogens <cite>Gordon-Thomson2009</cite>. A similar response is found in the tomato pathogen ''C. fulvum''; here, the effector protein utilizes CBM14's ability to bind chitin in the fungal cell wall enabling protection from hydrolysis by plant-derived chitinases during infection <cite>Joosten1997 Burg2006</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Although some of the structural features described above differ between the CBM14 lectins and CBM14<sub>CHIT1</sub>, the common denominator is the involvement of these modules in immune responses. CHIT1 is produced by macrophages and neutrophils <cite>Hollak1994, Kzhyshkowska2007</cite> and is utilized by the innate immune response to combat chitin-containing pathogens <cite>Gordon-Thomson2009</cite>. A similar response is found in the tomato pathogen ''C. fulvum''; here, the effector protein utilizes CBM14's ability to bind chitin in the fungal cell wall enabling protection from hydrolysis by plant-derived chitinases during infection <cite>Joosten1997 Burg2006</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>;First Identified: CBM14 was first identified as an antimicrobial lectin-like protein with chitin binding ability in the hemocyte of horseshoe crab (''Tachypleus tridentatus'') and called tachycitin <cite>Kawabata1996</cite>. </div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>;First Identified: CBM14 was first identified as an antimicrobial lectin-like protein with chitin<ins class="diffchange diffchange-inline">-</ins>binding ability in the hemocyte of horseshoe crab (''Tachypleus tridentatus'') and called tachycitin <cite>Kawabata1996</cite>. </div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First Structural Characterization: The first three-dimensional structure was determined by NMR spectroscopy for the CBM14 module tachycitin (PDB ID: [{{PDBlink}}1DQC 1DQC]) <cite>Suetake2000</cite>. The structure of the first carbohydrate-active enzyme associated CBM14 was determined by X-ray crystallography for the CBM14 of human chitotriosidase (PDB ID: [{{PDBlink}}5HBF 5HBF]) <cite>Fadel2016</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First Structural Characterization: The first three-dimensional structure was determined by NMR spectroscopy for the CBM14 module tachycitin (PDB ID: [{{PDBlink}}1DQC 1DQC]) <cite>Suetake2000</cite>. The structure of the first carbohydrate-active enzyme associated CBM14 was determined by X-ray crystallography for the CBM14 of human chitotriosidase (PDB ID: [{{PDBlink}}5HBF 5HBF]) <cite>Fadel2016</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
</table>Elizabeth Ficko-Blean