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

共 50 条

[21] Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1
GomisRuth, FX
Maskos, K
Betz, M
Bergner, A
Huber, R
Suzuki, K
Yoshida, N
Nagase, H
Brew, K
Bourenkov, GP
Bartunik, H
Bode, W
NATURE, 1997, 389 (6646) : 77 - 81
[22] IN-VITRO REGULATION OF STROMELYSIN-1 IN HUMAN ENDOMETRIAL STROMAL CELLS
SCHATZ, F
PAPP, C
TOTHPAL, E
AIGNER, S
HAUSKNECHT, V
KRIKUN, G
GORDON, RE
BERKOWITZ, R
LOCKWOOD, CJ
INHIBITION OF MATRIX METALLOPROTEINASES: THERAPEUTIC POTENTIAL, 1994, 732 : 479 - 481
[23] Solution structure of the catalytic domain of human collagenase-3 (MMP-13) complexed to a potent non-peptidic sulfonamide inhibitor: Binding comparison with stromelysin-1 and collagenase-1
Zhang, XL
Gonnella, NC
Koehn, J
Pathak, N
Ganu, V
Melton, R
Parker, D
Hu, SI
Nam, KY
JOURNAL OF MOLECULAR BIOLOGY, 2000, 301 (02) : 513 - 524
[24] A high throughput enzymatic assay for stromelysin-1
Pratta, MA
Blessington, DL
Trzaskos, JM
Arner, EC
INFLAMMATION RESEARCH, 1997, 46 : S118 - S119
[25] A high throughput enzymatic assay for stromelysin-1
M. A. Pratta
D. L. Blessington
J. M. Trzaskos
E. C. Arner
Inflammation Research, 1997, 46 (Suppl 2) : 118 - 119
[26] Role of his-224 in the anomalous pH dependence of human stromelysin-1
Holman, CM
Kan, CC
Gehring, MR
Van Wart, HE
BIOCHEMISTRY, 1999, 38 (02) : 677 - 681
[27] DIFFERENT DOMAIN INTERACTIONS ARE INVOLVED IN THE BINDING OF TISSUE INHIBITORS OF METALLOPROTEINASES TO STROMELYSIN-1 AND GELATINASE-A
NGUYEN, Q
WILLENBROCK, F
COCKETT, MI
OSHEA, M
DOCHERTY, AJP
MURPHY, G
BIOCHEMISTRY, 1994, 33 (08) : 2089 - 2095
[28] Role of stromelysin-1 in experimental acute lung injury
Johnson, KJ
Warner, RL
Varani, J
FASEB JOURNAL, 2002, 16 (04): : A590 - A590
[29] Inactivation of the serpin α2-antiplasmin by stromelysin-1
Lijnen, HR
Van Hoef, BT
Collen, D
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 2001, 1547 (02): : 206 - 213
[30] Analysis of the binding of hydroxamic acid and carboxylic acid inhibitors to the stromelysin-1 (matrix metalloproteinase-3) catalytic domain by isothermal titration calorimetry
Parker, MH
Lunney, EA
Ortwine, DF
Pavlovsky, AG
Humblet, C
Brouillette, CG
BIOCHEMISTRY, 1999, 38 (41) : 13592 - 13601

← 1 2 3 4 5 →