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1hoe
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(New page: 200px<br /><applet load="1hoe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hoe, resolution 2.0Å" /> '''CRYSTAL STRUCTURE DET...)
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Revision as of 14:35, 20 November 2007
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CRYSTAL STRUCTURE DETERMINATION, REFINEMENT AND THE MOLECULAR MODEL OF THE ALPHA-AMYLASE INHIBITOR HOE-467A
Overview
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.
About this Structure
1HOE is a Single protein structure of sequence from Streptomyces tendae. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Tue Nov 20 16:42:38 2007
