Crystal structure of the catalytic domain of human matrix metalloproteinase 10

被引：46

作者：

Bertini, I

Calderone, V

Fragai, M

Luchinat, C

Mangani, S

Terni, B

机构：

[1] Univ Florence, CERM, I-50019 Florence, Italy

[2] FiorGen Fdn, I-50019 Florence, Italy

[3] ProtEra Srl, I-50019 Florence, Italy

[4] Univ Siena, Dept Chem, I-53100 Siena, Italy

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2004年 / 336卷 / 03期

关键词：

matrix metalloproteinase; stromelysin-2; MMP-10; crystal structure; inhibitor;

D O I：

10.1016/j.jmb.2003.12.033

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 catalytic domain of matrix metalloproteinase-10 (MMP-10) has been expressed in Escherichia coli and its crystal structure solved at 2.1 Angstrom resolution. The availability of this structure allowed us to critically examine the small differences existing between the catalytic domains of MMP-3 and MMP-10, which show the highest sequence identity among all MMPs. Furthermore, the binding mode of N-isobutyl-N-[4-methoxy-phenylsulfonyl]glycyl hydroxamic acid (NNGH), which is one of the most known commercial inhibitors of MMPs, is described for the first time. (C) 2003 Elsevier Ltd. All rights reserved.

引用

页码：707 / 716

页数：10

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