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.
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页码：111 / 118
页数：8
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