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1hoe

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{{STRUCTURE_1hoe| PDB=1hoe | SCENE= }}
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'''CRYSTAL STRUCTURE DETERMINATION, REFINEMENT AND THE MOLECULAR MODEL OF THE ALPHA-AMYLASE INHIBITOR HOE-467A'''
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===CRYSTAL STRUCTURE DETERMINATION, REFINEMENT AND THE MOLECULAR MODEL OF THE ALPHA-AMYLASE INHIBITOR HOE-467A===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 3489104 is the PubMed ID number.
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{{ABSTRACT_PUBMED_3489104}}
==About this Structure==
==About this Structure==
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[[Category: Wiegand, G.]]
[[Category: Wiegand, G.]]
[[Category: Glycosidase inhibitor]]
[[Category: Glycosidase inhibitor]]
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Revision as of 05:28, 1 July 2008

Image:1hoe.png

Template:STRUCTURE 1hoe

CRYSTAL STRUCTURE DETERMINATION, REFINEMENT AND THE MOLECULAR MODEL OF THE ALPHA-AMYLASE INHIBITOR HOE-467A

Template:ABSTRACT PUBMED 3489104

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 Jul 1 08:28:04 2008

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