1BBS

X-RAY ANALYSES OF PEPTIDE INHIBITOR COMPLEXES DEFINE THE STRUCTURAL BASIS OF SPECIFICITY FOR HUMAN AND MOUSE RENINS

1BBS の概要

• エントリーDOI: 10.2210/pdb1bbs/pdb
• 分子名称: RENIN (1 entity in total)
• 機能のキーワード: aspartic 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: 2
• 化学式量合計: 74534.02

構造登録者

Dhanaraj, V.,Blundell, T.L. (登録日: 1992-05-21, 公開日: 1994-01-31, 最終更新日: 2024-11-06)

主引用文献

Dhanaraj, V.,Dealwis, C.G.,Frazao, C.,Badasso, M.,Sibanda, B.L.,Tickle, I.J.,Cooper, J.B.,Driessen, H.P.,Newman, M.,Aguilar, C.,Wood, S.P.,Blundell, T.L.,Hobart, P.M.,Geoghegan, K.F.,Ammirati, M.J.,Danley, D.E.
X-ray analyses of peptide-inhibitor complexes define the structural basis of specificity for human and mouse renins.
Nature, 357:466-472, 1992

PubMed Abstract: X-ray analyses have defined the three-dimensional structures of crystals of mouse and human renins complexed with peptide inhibitors at resolutions of 1.9 and 2.8 A, respectively. The exquisite specificity of renin arises partly from ordered loop regions at the periphery of the binding cleft. Although the pattern of main-chain hydrogen bonding in other aspartic proteinase inhibitor complexes is conserved in renins, differences in the positions of secondary structure elements (particularly helices) also lead to improved specificity in renins for angiotensinogen substrates.

PubMed: 1608447
DOI: 10.1038/357466a0

実験手法

X-RAY DIFFRACTION (2.8 Å)