1r1j

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Image:1r1j.gif

1r1j, resolution 2.35Å

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STRUCTURAL ANALYSIS OF NEPRILYSIN WITH VARIOUS SPECIFIC AND POTENT INHIBITORS

Contents

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. Owing, to the physiological importance of NEP in the modulation of nociceptive, and pressor responses, there is considerable interest in inhibitors of, this enzyme as novel analgesics and antihypertensive agents. Here, the, crystal structures of the soluble extracellular domain of human NEP, (residues 52-749) complexed with various potent and competitive inhibitors, are described. The structures unambiguously reveal the binding mode of the, different zinc-chelating groups and the subsite specificity of the enzyme.

Disease

Known diseases associated with this structure: Membranous glomerulonephritis, antenatal OMIM:[120520], Neutral endopeptidase deficiency OMIM:[120520], Schizophrenia, susceptibility to OMIM:[607265]

About this Structure

1R1J is a Single protein structure of sequence from Homo sapiens with NAG, ZN and OIR as ligands. Active as Neprilysin, with EC number 3.4.24.11 Full crystallographic information is available from OCA.

Reference

Structural analysis of neprilysin with various specific and potent inhibitors., Oefner C, Roques BP, Fournie-Zaluski MC, Dale GE, Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):392-6. Epub 2004, Jan 23. PMID:14747736

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