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Crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor Hoe-467A.

作者信息

Pflugrath J W, Wiegand G, Huber R, Vértesy L

出版信息

J Mol Biol. 1986 May 20;189(2):383-6. doi: 10.1016/0022-2836(86)90520-6.

DOI:10.1016/0022-2836(86)90520-6
PMID:3489104
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.

摘要

相似文献

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Crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor Hoe-467A.
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