1BIM

CRYSTALLOGRAPHIC STUDIES ON THE BINDING MODES OF P2-P3 BUTANEDIAMIDE RENIN INHIBITORS

1BIM の概要

• エントリーDOI: 10.2210/pdb1bim/pdb
• 分子名称: Renin, (2S)-2-[(2-amino-1,3-thiazol-4-yl)methyl]-N~1~-{(1S,2S)-1-(cyclohexylmethyl)-2-hydroxy-2-[(3R)-1,5,5-trimethyl-2-oxopyrrolidin-3-yl]ethyl}-N~4~-[2-(dimethylamino)-2-oxoethyl]-N~4~-[(1S)-1-phenylethyl]butanediamide (2 entities in total)
• 機能のキーワード: aspartic proteinase, aspartyl protease, cleavage on pair of basic residues, disease mutation, disulfide bond, glycoprotein, hydrolase, membrane, protease, secreted, zymogen, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75245.02

構造登録者

Tong, L. (登録日: 1995-09-27, 公開日: 1996-01-29, 最終更新日: 2024-10-16)

主引用文献

Tong, L.,Pav, S.,Lamarre, D.,Simoneau, B.,Lavallee, P.,Jung, G.
Crystallographic studies on the binding modes of P2-P3 butanediamide renin inhibitors.
J.Biol.Chem., 270:29520-29524, 1995

PubMed Abstract: The binding modes of three peptidomimetic P2-P3 butanediamide renin inhibitors have been determined by x-ray crystallography. The inhibitors are bound with their backbones in an extended conformation, and their side chains occupying the S5 to S1' pockets. A (2-amino-4-thiazolyl)methyl side chain at the P2 position shows stronger hydrogen-bonding and van der Waals interactions with renin than the His side chain, which is present in the natural substrate. The ACHPA-gamma-lactam transition state analog has similar interactions with renin as the dihydroxyethylene transition state analog.

PubMed: 7493993
DOI: 10.1074/jbc.270.49.29520

実験手法

X-RAY DIFFRACTION (2.8 Å)