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

被引：127

作者：

DHANARAJ, V

DEALWIS, CG

FRAZAO, C

BADASSO, M

SIBANDA, BL

TICKLE, IJ

COOPER, JB

DRIESSEN, HPC

NEWMAN, M

AGUILAR, C

WOOD, SP

BLUNDELL, TL

HOBART, PM

GEOGHEGAN, KF

AMMIRATI, MJ

DANLEY, DE

OCONNOR, BA

HOOVER, DJ

机构：

[1] UNIV LONDON BIRKBECK COLL,MOLEC BIOL LAB,LONDON WC1E 7HX,ENGLAND

[2] UNIV LONDON BIRKBECK COLL,DEPT CRYSTALLOG,IMPERIAL CANC RES FUND,STRUCT MOLEC BIOL UNIT,LONDON WC1E 7HX,ENGLAND

[3] PFIZER INC,DEPT MOLEC GENET & PROT CHEM,GROTON,CT 06340

[4] PFIZER INC,DEPT MED CHEM,DIV CENT RES,GROTON,CT 06340

来源：

NATURE | 1992年 / 357卷 / 6378期

关键词：

D O I：

10.1038/357466a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 angstrom, 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.

引用

页码：466 / 472

页数：7

共 36 条

[1] 3-DIMENSIONAL STRUCTURE OF HUMAN RENIN [J].