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Difference between revisions of "Carbohydrate Binding Module Family 94"
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== Family Firsts == | == Family Firsts == | ||
;First Identified | ;First Identified | ||
| − | : | + | :Sugar-binding ability of the C-terminal domains of human and mouse GnT-IVa (MGAT4A) and ''Bombyx mori'' ortholog was identified independently by two groups <cite>Oka2022,Nagae2022</cite>. |
;First Structural Characterization | ;First Structural Characterization | ||
| − | : | + | :Crystal structures of the C-terminal domains of human and mouse GnT-IVa (MGAT4A) and ''Bombyx mori'' ortholog were determined independently by two groups <cite>Oka2022,Nagae2022</cite>. β-GlcNAc-bound structure of ''B. mori'' CBM94 was also determined <cite>Oka2022</cite>. |
== References == | == References == | ||
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#Osada2022 pmid=35988645 | #Osada2022 pmid=35988645 | ||
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</biblio> | </biblio> | ||
<!-- Do not delete this Category tag --> | <!-- Do not delete this Category tag --> | ||
[[Category:Carbohydrate Binding Module Families|CBM094]] | [[Category:Carbohydrate Binding Module Families|CBM094]] | ||
Revision as of 19:31, 10 January 2023
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/CBM94.html |
Ligand specificities
Mention here all major natural ligand specificities that are found within a given family (also plant or mammalian origin). Certain linkages and promiscuity would also be mentioned here if biologically relevant.
Note: Here is an example of how to insert references in the text, together with the "biblio" section below: Please see these references for an essential introduction to the CAZy classification system: [1, 2]. CBMs, in particular, have been extensively reviewed [3, 4, 5, 6, 7].
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
- Sugar-binding ability of the C-terminal domains of human and mouse GnT-IVa (MGAT4A) and Bombyx mori ortholog was identified independently by two groups [8, 9].
- First Structural Characterization
- Crystal structures of the C-terminal domains of human and mouse GnT-IVa (MGAT4A) and Bombyx mori ortholog were determined independently by two groups [8, 9]. β-GlcNAc-bound structure of B. mori CBM94 was also determined [8].
References
- Oka N, Mori S, Ikegaya M, Park EY, and Miyazaki T. (2022). Crystal structure and sugar-binding ability of the C-terminal domain of N-acetylglucosaminyltransferase IV establish a new carbohydrate-binding module family. Glycobiology. 2022;32(12):1153-1163. DOI:10.1093/glycob/cwac058 |
- Nagae M, Hirata T, Tateno H, Mishra SK, Manabe N, Osada N, Tokoro Y, Yamaguchi Y, Doerksen RJ, Shimizu T, and Kizuka Y. (2022). Discovery of a lectin domain that regulates enzyme activity in mouse N-acetylglucosaminyltransferase-IVa (MGAT4A). Commun Biol. 2022;5(1):695. DOI:10.1038/s42003-022-03661-w |
- Osada N, Nagae M, Nakano M, Hirata T, and Kizuka Y. (2022). Examination of differential glycoprotein preferences of N-acetylglucosaminyltransferase-IV isozymes a and b. J Biol Chem. 2022;298(9):102400. DOI:10.1016/j.jbc.2022.102400 |