1xgl
From Proteopedia
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==Overview== | ==Overview== | ||
| - | We have determined the structure of a metastable disulphide isomer of | + | 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. |
==Disease== | ==Disease== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Chance, R | + | [[Category: Chance, R E.]] |
| - | [[Category: Frank, B | + | [[Category: Frank, B H.]] |
| - | [[Category: Gozani, S | + | [[Category: Gozani, S N.]] |
| - | [[Category: Hoffmann, J | + | [[Category: Hoffmann, J A.]] |
| - | [[Category: Hua, Q | + | [[Category: Hua, Q X.]] |
| - | [[Category: Weiss, M | + | [[Category: Weiss, M A.]] |
[[Category: glucose metabolism]] | [[Category: glucose metabolism]] | ||
[[Category: hormone]] | [[Category: hormone]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:54:33 2008'' |
Revision as of 13:54, 21 February 2008
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HUMAN INSULIN DISULFIDE ISOMER, NMR, 10 STRUCTURES
Contents |
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.
Disease
Known diseases associated with this structure: Diabetes mellitus, rare form OMIM:[176730], Hyperproinsulinemia, familial OMIM:[176730], MODY, one form OMIM:[176730]
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 Thu Feb 21 15:54:33 2008
