User:Cboursnell/Sandbox/A amylase inhib
| A_amylase_inhib | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor hoe-467a | |||||||||
| Identifiers | |||||||||
| Symbol | A_amylase_inhib | ||||||||
| Pfam | PF01356 | ||||||||
| InterPro | IPR000833 | ||||||||
| SCOP2 | 1hoe / SCOPe / SUPFAM | ||||||||
| |||||||||
Alpha-amylase inhibitor inhibits mammalian alpha-amylases specifically, by forming a tight stoichiometric 1:1 complex with alpha-amylase. The inhibitor 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.[1] 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.
More information about this protein can be found at Protein of the Month: alpha-Amylase .
References
[edit]- ^ König V, Vértesy L, Schneider TR (October 2003). "Structure of the alpha-amylase inhibitor tendamistat at 0.93 A". Acta Crystallogr. D Biol. Crystallogr. 59 (Pt 10): 1737–1743. doi:10.1107/s0907444903015828. PMID 14501112.
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