1hoe

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[[Image:1hoe.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hoe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hoe OCA], [http://www.ebi.ac.uk/pdbsum/1hoe PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hoe RCSB]</span>
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'''CRYSTAL STRUCTURE DETERMINATION, REFINEMENT AND THE MOLECULAR MODEL OF THE ALPHA-AMYLASE INHIBITOR HOE-467A'''
'''CRYSTAL STRUCTURE DETERMINATION, REFINEMENT AND THE MOLECULAR MODEL OF THE ALPHA-AMYLASE INHIBITOR HOE-467A'''
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[[Category: Pflugrath, J W.]]
[[Category: Pflugrath, J W.]]
[[Category: Wiegand, G.]]
[[Category: Wiegand, G.]]
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[[Category: glycosidase inhibitor]]
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[[Category: Glycosidase inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:04:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:08:19 2008''
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Revision as of 16:04, 2 May 2008

Image:1hoe.gif

Template:STRUCTURE 1hoe

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 Fri May 2 19:04:04 2008

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