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2hiu
From Proteopedia
NMR STRUCTURE OF HUMAN INSULIN IN 20% ACETIC ACID, ZINC-FREE, 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
2HIU is a Protein complex structure of sequences from Homo sapiens. This structure supersedes the now removed PDB entry 1hiu. The following page contains interesting information on the relation of 2HIU with [Insulin]. 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 Sun May 4 06:20:47 2008
