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1lph

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[[Category: insulin analogue]]
[[Category: insulin analogue]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:16:07 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:42:33 2007''

Revision as of 13:37, 30 October 2007

Image:1lph.gif

1lph, resolution 2.3Å

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LYS(B28)PRO(B29)-HUMAN INSULIN

Overview

BACKGROUND: LysB28ProB29-human insulin (Humalog), a fully potent insulin, analog in which the prolyl, lysyl sequence at the C-terminal end of the, B-chain is inverted, exhibits a decreased association of monomers to, dimers leading to rapid in vivo absorption. This provides important, benefits for the insulin-requiring diabetic. In spite of its monomeric, nature, LysB28ProB29-human insulin can exist as a discrete hexameric, structure in the presence of both zinc and phenol. Studies of the crystal, structure of LysB28ProB29-human insulin in a hexameric complex were, initiated to gain a molecular understanding of the effect of the sequence, inversion on the analog's self-association properties and, consequently, its in vivo efficacy. RESULTS: Under the conditions reported, ... [(full description)]

About this Structure

1LPH is a [Protein complex] structure of sequences from [Homo sapiens] with ZN, CL and IPH as [ligands]. Structure known Active Site: 1. Full crystallographic information is available from [OCA].

Reference

Role of C-terminal B-chain residues in insulin assembly: the structure of hexameric LysB28ProB29-human insulin., Ciszak E, Beals JM, Frank BH, Baker JC, Carter ND, Smith GD, Structure. 1995 Jun 15;3(6):615-22. PMID:8590022

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