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2hiu

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(New page: 200px<br /> <applet load="2hiu" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hiu" /> '''NMR STRUCTURE OF HUMAN INSULIN IN 20% ACETI...)
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Revision as of 20:26, 12 November 2007


2hiu

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NMR STRUCTURE OF HUMAN INSULIN IN 20% ACETIC ACID, ZINC-FREE, 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

2HIU is a Protein complex structure of sequences from Homo sapiens. This structure superseeds 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 Mon Nov 12 22:33:07 2007

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