Structural highlights
Function
[IAA_STRTE] Inhibits mammalian alpha-amylases specifically but has no action on plant and microbial alpha-amylases. Forms a tight stoichiometric 1:1 complex with alpha-amylase.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal and molecular structure of the alpha-amylase inhibitor Hoe-467A has been determined and refined at high resolution. The polypeptide chain is folded in two triple-stranded sheets, which form a barrel. The topology of folding is as found in the immunoglobulin domains. The amino acid triplet Trp18-Arg19-Tyr20 has an exceptional conformation and position in the molecule and is possibly involved in inhibitory activity.
Crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor Hoe-467A.,Pflugrath JW, Wiegand G, Huber R, Vertesy L J Mol Biol. 1986 May 20;189(2):383-6. PMID:3489104[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pflugrath JW, Wiegand G, Huber R, Vertesy L. Crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor Hoe-467A. J Mol Biol. 1986 May 20;189(2):383-6. PMID:3489104
