Difference between revisions of "Carbohydrate Binding Module Family 14"

Revision as of 07:07, 26 November 2020

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.

Author: ^^^Eva Madland^^^
Responsible Curator: ^^^Elizabeth Ficko-Blean^^^

CAZy DB link
https://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] Members of CBM14 have been shown to bind chitin [5, 6, 7] and chitooligomers. [3, 8] Binding to 50 % acetylated hyaluronan has also been demonstrated. [8]

The ligand binding affinities have been quantified for two CBM14 members. The interaction between a human chitotriosidase-1 (CHIT1, characterized as a glycoside hydrolase family 18 (GH18)) CBM14 and (GlcNAc)₃ have been investigated with NMR titration experiments and isothermal titration calorimetry (ITC) displaying a relatively weak interaction of K_d 9.9 ± 0.8 mM [8] and K_d 3.1 ± 0.2 mM [7], respectively.

Interaction studies have also been performed for CBM14 in the fungal tomato pathogen C. fulvum and (GlcNAc)₆. Here, the binding properties were measured using ITC yielding a K_d of 6.7 ± 1.5 uM. [3]

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

All Medline abstracts: PubMed

@@ Line 20: / Line 20: @@
 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> 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>
-The ligand binding affinities have been quantified for two CBM14 members. The interaction between a human chitotriosidase-1 (CHIT1, characterized as a glycoside hydrolase family 18 ([[GH18]])) CBM14 and (GlcNAc)<sub>3</sub> have been investigated with NMR titration experiments and isothermal titration calorimetry (ITC) displaying a relatively weak interaction of K<sub>d</sub> 9.9 0.8 mM  <cite>Crasson2016</cite> and K<sub>d</sub> 3.1 0.2 mM  <cite>Madland2019</cite>, respectively.
+The ligand binding affinities have been quantified for two CBM14 members. The interaction between a human chitotriosidase-1 (CHIT1, characterized as a glycoside hydrolase family 18 ([[GH18]])) CBM14 and (GlcNAc)<sub>3</sub> have been investigated with NMR titration experiments and isothermal titration calorimetry (ITC) displaying a relatively weak interaction of K<sub>d</sub> 9.9 &plusmn; 0.8 mM  <cite>Crasson2016</cite> and K<sub>d</sub> 3.1 &plusmn; 0.2 mM  <cite>Madland2019</cite>, respectively.
-Interaction studies have also been performed for CBM14 in the fungal tomato pathogen ''C. fulvum'' and (GlcNAc)<sub>6</sub>. Here, the binding properties were measured using ITC yielding a K<sub>d</sub> of 6.7 1.5 uM. <cite>Hurlburt2018</cite>
+Interaction studies have also been performed for CBM14 in the fungal tomato pathogen ''C. fulvum'' and (GlcNAc)<sub>6</sub>. Here, the binding properties were measured using ITC yielding a K<sub>d</sub> of 6.7 &plusmn; 1.5 uM. <cite>Hurlburt2018</cite>
 == Structural Features ==