Alpha amylase inhibitor
| A_amylase_inhib | |||||||||
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crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor hoe-467a
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| Identifiers | |||||||||
| Symbol | A_amylase_inhib | ||||||||
| Pfam | PF01356 | ||||||||
| InterPro | IPR000833 | ||||||||
| SCOP | 1hoe | ||||||||
| SUPERFAMILY | 1hoe | ||||||||
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| Available protein structures: | |
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| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
In molecular biology, alpha-amylase inhibitor is a protein family which inhibits mammalian alpha-amylases specifically, by forming a tight stoichiometric 1:1 complex with alpha-amylase. This family of inhibitors has no action on plant and microbial alpha amylases.
A crystal structure has been determined for tendamistat, the 74-amino acid inhibitor produced by Streptomyces tendae that targets a wide range of mammalian alpha-amylases. The binding of tendamistat to alpha-amylase leads to the steric blockage of the active site of the enzyme. The crystal structure of tendamistat revealed an immunoglobulin-like fold that could potentially adopt multiple conformations. Such molecular flexibility could enable an induced-fit type of binding that would both optimise binding and allow broad target specificity.
This article incorporates text from the public domain Pfam and InterPro IPR000833
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