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2qpj

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(New page: 200px<br /><applet load="2qpj" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qpj, resolution 2.05&Aring;" /> '''Human NEP complexed ...)
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Revision as of 09:59, 23 January 2008

Image:2qpj.jpg

2qpj, resolution 2.05Å

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Human NEP complexed with a bifunctional NEP/DPP IV inhibitor

Overview

Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic, inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well, as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent, stimulator of insulin secretion. The activity of GLP-1 is also rapidly, abolished by the serine protease dipeptidyl peptidase IV (DPP-IV), which, led to an elevated interest in inhibitors of this enzyme for the treatment, of type II diabetes. A dual NEP/DPP-IV inhibitor concept is proposed, offering an alternative strategy for the treatment of type 2 diabetes., Here, the synthesis and crystal structures of the soluble extracellular, domain of human NEP (residues 52-749) complexed with the NEP, competitive, and potent dual NEP/DPP-IV inhibitor MCB3937 are described.

About this Structure

2QPJ is a Single protein structure of sequence from Homo sapiens with , and as ligands. Active as Neprilysin, with EC number 3.4.24.11 Full crystallographic information is available from OCA.

Reference

Structural studies of a bifunctional inhibitor of neprilysin and DPP-IV., Oefner C, Pierau S, Schulz H, Dale GE, Acta Crystallogr D Biol Crystallogr. 2007 Sep;63(Pt 9):975-81. Epub 2007, Aug 17. PMID:17704566

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