1R1H

STRUCTURAL ANALYSIS OF NEPRILYSIN WITH VARIOUS SPECIFIC AND POTENT INHIBITORS

1R1H の概要

• エントリーDOI: 10.2210/pdb1r1h/pdb
• 関連するPDBエントリー: 1DMT 1R1I 1R1J
• 分子名称: Neprilysin, 2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (5 entities in total)
• 機能のキーワード: enkephalinase, glycoprotein, metalloprotease, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane; Single-pass type II membrane protein: P08473
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 80672.96

構造登録者

Oefner, C.,Roques, B.P.,Fournie-Zaluski, M.C.,Dale, G.E. (登録日: 2003-09-24, 公開日: 2004-09-28, 最終更新日: 2024-11-20)

主引用文献

Oefner, C.,Roques, B.P.,Fournie-Zaluski, M.C.,Dale, G.E.
Structural analysis of neprilysin with various specific and potent inhibitors.
Acta Crystallogr.,Sect.D, 60:392-396, 2004

PubMed Abstract: 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.

PubMed: 14747736
DOI: 10.1107/S0907444903027410

実験手法

X-RAY DIFFRACTION (1.95 Å)