2REN

STRUCTURE OF RECOMBINANT HUMAN RENIN, A TARGET FOR CARDIOVASCULAR-ACTIVE DRUGS, AT 2.5 ANGSTROMS RESOLUTION

2REN の概要

• エントリーDOI: 10.2210/pdb2ren/pdb
• 分子名称: RENIN, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• 機能のキーワード: hydrolase(acid proteinase)
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P00797
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37488.22

構造登録者

Sielecki, A.R.,James, M.N.G. (登録日: 1992-02-05, 公開日: 1994-01-31, 最終更新日: 2024-11-06)

主引用文献

Sielecki, A.R.,Hayakawa, K.,Fujinaga, M.,Murphy, M.E.,Fraser, M.,Muir, A.K.,Carilli, C.T.,Lewicki, J.A.,Baxter, J.D.,James, M.N.
Structure of recombinant human renin, a target for cardiovascular-active drugs, at 2.5 A resolution.
Science, 243:1346-1351, 1989

PubMed Abstract: The x-ray crystal structure of recombinant human renin has been determined. Molecular dynamics techniques that included crystallographic data as a restraint were used to improve an initial model based on porcine pepsinogen. The present agreement factor for data from 8.0 to 2.5 angstroms (A) is 0.236. Some of the surface loops are poorly determined, and these disordered regions border a 30 A wide solvent channel. Comparison of renin with other aspartyl proteinases shows that, although the structural cores and active sites are highly conserved, surface residues, some of which are critical for specificity, vary greatly (up to 10A). Knowledge of the actual structure, as opposed to the use of models based on related enzymes, should facilitate the design of renin inhibitors.

PubMed: 2493678

実験手法

X-RAY DIFFRACTION (2.5 Å)