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Carbohydrate-binding module family 10 (CBM10) is found in two distinct sets of proteins with different functions. Those found in aerobic bacteria bind cellulose (or other carbohydrates); but in anaerobic fungi they are protein binding domains, referred to as dockerin domains .
HexB is structurally similar to chitobiase, consisting of a beta sandwich structure; this structure is similar to that found in the cellulose-binding domain of cellulase from Cellulomonas fimi. [1] This domain may function as a carbohydrate binding module.
These interactions form the basis of specific recognition of carbohydrates by lectins. Carbohydrates are important biopolymers and have a variety of functions. Often carbohydrates serve a function as a recognition element. That is, they are specifically recognized by other biomolecules. Proteins which bind carbohydrate structures are known as ...
Carbohydrate-responsive element-binding protein (ChREBP) also known as MLX-interacting protein-like (MLXIPL) is a protein that in humans is encoded by the MLXIPL gene. [ 5 ] [ 6 ] The protein name derives from the protein's interaction with carbohydrate response element sequences of DNA.
Algal cellulases are modular, consisting of putative novel cysteine-rich carbohydrate-binding modules (CBMs), proline/serine-(PS) rich linkers in addition to putative Ig-like and unknown domains in some members. Cellulase from Gonium pectorale consisted of two CDs separated by linkers and with a C-terminal CBM. [6]
These enzymes are of considerable biological and industrial importance. Gilbert has used structure-function studies to dissect the contribution of non-catalytic carbohydrate binding modules (CBMs) [5] in targeting enzymes to complex insoluble structures exemplified by the plant cell wall, thereby overcoming the access problem. [6] [7]
Each selectin has a carbohydrate recognition domain that mediates binding to specific glycans on apposing cells. They have remarkably similar protein folds and carbohydrate binding residues, [1] leading to overlap in the glycans to which they bind. Selectins bind to the sialyl Lewis X (SLe x) determinant “NeuAcα2-3Galβ1-4(Fucα1-3)GlcNAc.”
This domain is involved in carbohydrate binding. [1] Structure. The X8 domain [2] contains 6 conserved cysteine residues that presumably form three disulphide bridges.