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CHB HEX N-terminal domain
| Field | Value |
|---|---|
| Symbol | CHB_HEX |
| Name | CHB HEX N-terminal domain |
| image | PDB 1c7t EBI.jpg |
| caption | beta-n-acetylhexosaminidase mutant e540d complexed with di-n acetyl-d-glucosamine (chitobiase) |
| Pfam | PF03173 |
| Pfam_clan | CL0203 |
| InterPro | IPR004866 |
| SCOP | 1c7s |
In molecular biology, the CHB HEX N-terminal domain represents the N-terminal domain in chitobiases and beta-hexosaminidases. Chitobiases degrade chitin, which forms the exoskeleton in insects and crustaceans, and which is one of the most abundant polysaccharides on earth. Beta-hexosaminidases are composed of either a HexA/HexB heterodimer or a HexB homodimer, and can hydrolyse diverse substrates, including GM(2)-gangliosides; mutations in this enzyme are associated with Tay–Sachs disease. 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. This domain may function as a carbohydrate binding module.
References
References
- (July 1996). "Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay–Sachs disease". Nat. Struct. Biol..
- (April 2003). "Crystal structure of human beta-hexosaminidase B: understanding the molecular basis of Sandhoff and Tay–Sachs disease". J. Mol. Biol..
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