Biology:CHB HEX N-terminal domain
| CHB HEX N-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 beta-n-acetylhexosaminidase mutant e540d complexed with di-n acetyl-d-glucosamine (chitobiase) | |||||||||
| Identifiers | |||||||||
| Symbol | CHB_HEX | ||||||||
| Pfam | PF03173 | ||||||||
| Pfam clan | CL0203 | ||||||||
| InterPro | IPR004866 | ||||||||
| SCOP2 | 1c7s / SCOPe / SUPFAM | ||||||||
| |||||||||
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.[1] 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.[2] 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.
References
- ↑ 1.0 1.1 "Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay–Sachs disease". Nat. Struct. Biol. 3 (7): 638–48. July 1996. doi:10.1038/nsb0796-638. PMID 8673609.
- ↑ "Crystal structure of human beta-hexosaminidase B: understanding the molecular basis of Sandhoff and Tay–Sachs disease". J. Mol. Biol. 327 (5): 1093–109. April 2003. doi:10.1016/S0022-2836(03)00216-X. PMID 12662933.
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