1xda

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Revision as of 17:57, 12 November 2007

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spinqualitylabelsall models 1xda, resolution 1.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURE OF INSULIN

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

The fatty acid acylated insulin, Lys(B29)-tetradecanoyl, des-(B30) human, insulin, has been crystallized and the structure determined by X-ray, crystallography. The fatty acid substituent on residue B29 Lys binds, reversibly to circulating albumin protein in vivo, and by this mechanism, the hormone's action is prolonged. Crystals of the fatty acid insulin grow, in space group R3, with two dimers in the asymmetric unit, and diffract to, 1.8 A spacing. The structure has been solved by molecular replacement and, refined using a maximum likelihood method. The crystal structure consists, of R6 zinc insulin hexamers which contain phenol. The fatty acids can be, seen bound between the hexamers, making specific interactions with the, side chains of residue B1 Phe; however, the lysine side chains to which, the fatty acids are covalently attached are mostly disordered. The mode of, binding of the fatty acids appears to be determined by crystal packing, and whether or not they interact with the protein in this way in solution, remains uncertain.

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

1XDA is a Protein complex structure of sequences from Homo sapiens with ZN, CL, IPH and MYR as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of a prolonged-acting insulin with albumin-binding properties., Whittingham JL, Havelund S, Jonassen I, Biochemistry. 1997 Mar 11;36(10):2826-31. PMID:9062110

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