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Difference between revisions of "Carbohydrate Binding Module Family 14"

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== Ligand specificities ==
 
== Ligand specificities ==
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. an effector protein from the tomato pathogen Pseudoercospora fuligena or Cladosporium fulvum  
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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. an effector protein from the tomato pathogen ''Pseudoercospora fuligena'' or ''Cladosporium fulvum''<cite>Kohler2016 Hurlburt2018</cite>, as an antimicrobial lectin-like protein from horseshoe crab haemocytes (tachycitin) <cite>Kawabata1996</cite> and in peritrophic matrix proteins from Malaria vector ''Anopheles gambia''. <cite>Shen1998</cite>
  
  
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<biblio>
 
<biblio>
 
#Fadel2016 pmid=27111557
 
#Fadel2016 pmid=27111557
 
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#Kohler2016 pmid: 27401545
 
+
#Hurlburt2018 pmid: 30148881
 +
#Kawabata1996 pmid: 9010778
 +
#Shen1998 pmid: 9651363
 +
#Vandevenne2011 pmid: 21674664
 +
#Madland2019 pmid: 31891077
 +
#Crasson2016 pmid: 28584264
 +
#Suetake2000 pmid: 10770921
 
#Boraston2004 pmid=15214846
 
#Boraston2004 pmid=15214846
  

Revision as of 06:37, 26 November 2020

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This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.


CAZy DB link
http://www.cazy.org/CBMnn.html

Ligand specificities

Family 14 CBMs are modules composed of approximately 70 residues. These modules have been reported to be associated with chitinases [1] and as chitin-binding lectins e.g. an effector protein from the tomato pathogen Pseudoercospora fuligena or Cladosporium fulvum[2, 3], as an antimicrobial lectin-like protein from horseshoe crab haemocytes (tachycitin) [4] and in peritrophic matrix proteins from Malaria vector Anopheles gambia. [5]


Structural Features

Content in this section should include, in paragraph form, a description of:

  • Fold: Structural fold (beta trefoil, beta sandwich, etc.)
  • Type: Include here Type A, B, or C and properties
  • Features of ligand binding: Describe CBM binding pocket location (Side or apex) important residues for binding (W, Y, F, subsites), interact with reducing end, non-reducing end, planar surface or within polysaccharide chains. Include examples pdb codes. Metal ion dependent. Etc.

Functionalities

Content in this section should include, in paragraph form, a description of:

  • Functional role of CBM: Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.
  • Most Common Associated Modules: 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)
  • Novel Applications: Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.

Family Firsts

First Identified
Insert archetype here, possibly including very brief synopsis.
First Structural Characterization
Insert archetype here, possibly including very brief synopsis.

References

  1. Fadel F, Zhao Y, Cousido-Siah A, Ruiz FX, Mitschler A, and Podjarny A. (2016). X-Ray Crystal Structure of the Full Length Human Chitotriosidase (CHIT1) Reveals Features of Its Chitin Binding Domain. PLoS One. 2016;11(4):e0154190. DOI:10.1371/journal.pone.0154190 | PubMed ID:27111557 [Fadel2016]
  2. pmid: 27401545

    [Kohler2016]
  3. pmid: 30148881

    [Hurlburt2018]
  4. pmid: 9010778

    [Kawabata1996]
  5. pmid: 9651363

    [Shen1998]
  6. pmid: 21674664

    [Vandevenne2011]
  7. pmid: 31891077

    [Madland2019]
  8. pmid: 28584264

    [Crasson2016]
  9. pmid: 10770921

    [Suetake2000]
  10. Boraston AB, Bolam DN, Gilbert HJ, and Davies GJ. (2004). Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem J. 2004;382(Pt 3):769-81. DOI:10.1042/BJ20040892 | PubMed ID:15214846 [Boraston2004]

All Medline abstracts: PubMed