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1xgl

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xgl OCA], [http://www.ebi.ac.uk/pdbsum/1xgl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xgl RCSB]</span>
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'''HUMAN INSULIN DISULFIDE ISOMER, NMR, 10 STRUCTURES'''
'''HUMAN INSULIN DISULFIDE ISOMER, NMR, 10 STRUCTURES'''
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[[Category: Hua, Q X.]]
[[Category: Hua, Q X.]]
[[Category: Weiss, M A.]]
[[Category: Weiss, M A.]]
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[[Category: glucose metabolism]]
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[[Category: Glucose metabolism]]
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[[Category: hormone]]
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[[Category: Hormone]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:00:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:49:19 2008''
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Revision as of 12:00, 3 May 2008

Template:STRUCTURE 1xgl

HUMAN INSULIN DISULFIDE ISOMER, NMR, 10 STRUCTURES


Overview

We have determined the structure of a metastable disulphide isomer of human insulin. Although not observed for proinsulin folding or insulin-chain recombination, the isomer retains ordered secondary structure and a compact hydrophobic core. Comparison with native insulin reveals a global rearrangement in the orientation of A- and B-chains. One face of the protein's surface is nevertheless in common between native and non-native structures. This face contains receptor-binding determinants, rationalizing the partial biological activity of the isomer. Structures of native and non-native disulphide isomers also define alternative three-dimensional templates. Threading of insulin-like sequences provide an experimental realization of the inverse protein-folding problem.

About this Structure

1XGL is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of a protein in a kinetic trap., Hua QX, Gozani SN, Chance RE, Hoffmann JA, Frank BH, Weiss MA, Nat Struct Biol. 1995 Feb;2(2):129-38. PMID:7749917 Page seeded by OCA on Sat May 3 15:00:16 2008

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