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1xgl
From Proteopedia
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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: | + | [[Category: Hormone]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:00:16 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 12:00, 3 May 2008
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
