1xgl
HUMAN INSULIN DISULFIDE ISOMER, NMR, 10 STRUCTURES
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OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Diabetes mellitus, rare form OMIM:[176730], Hyperproinsulinemia, familial OMIM:[176730], MODY, one form OMIM:[176730]
About this StructureAbout this Structure
1XGL is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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