THE NMR STRUCTURE OF THE INHIBITED CATALYTIC DOMAIN OF HUMAN STROMELYSIN-1

被引：132

作者：

GOOLEY, PR ^{[1
]}

OCONNELL, JF ^{[1
]}

MARCY, AI ^{[1
]}

CUCA, GC ^{[1
]}

SALOWE, SP ^{[1
]}

BUSH, BL ^{[1
]}

HERMES, JD ^{[1
]}

ESSER, CK ^{[1
]}

HAGMANN, WK ^{[1
]}

SPRINGER, JP ^{[1
]}

JOHNSON, BA ^{[1
]}

机构：

[1] MERCK & CO INC,MERCK SHARP & DOHME RES LABS,DEPT MED CHEM RES,RAHWAY,NJ 07065

来源：

NATURE STRUCTURAL BIOLOGY | 1994年 / 1卷 / 02期

关键词：

D O I：

10.1038/nsb0294-111

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The three-dimensional structure of the catalytic domain of stromelysin-1 complexed with an N-carboxyl alkyl inhibitor has been determined by NMR methods. The global fold consists of three helices, a five stranded beta-sheet and a methionine located in a turn near the catalytic histidines, classifying stromelysin-1 as a metzincin. Stromelysin-1 is unique in having two independent zinc binding sites: a catalytic site and a structural site. The inhibitor binds in an extended conformation. The S1' subsite is a deep hydrophobic pocket, whereas S2' appears shallow and 53' open.

引用

页码：111 / 118

页数：8

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