| Literature DB >> 3489104 |
J W Pflugrath, G Wiegand, R Huber, L Vértesy.
Abstract
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.Entities:
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Year: 1986 PMID: 3489104 DOI: 10.1016/0022-2836(86)90520-6
Source DB: PubMed Journal: J Mol Biol ISSN: 0022-2836 Impact factor: 5.469