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Crystal Structure of the Catalytic Domain of Human Matrix Metalloproteinase 10

Authors :
Vito Calderone
Marco Fragai
Stefano Mangani
Beatrice Terni
Claudio Luchinat
Ivano Bertini
Source :
Journal of Molecular Biology. 336:707-716
Publication Year :
2004
Publisher :
Elsevier BV, 2004.

Abstract

The catalytic domain of matrix metalloproteinase-10 (MMP-10) has been expressed in Escherichia coli and its crystal structure solved at 2.1 A 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-methoxyphenylsulfonyl]glycyl hydroxamic acid (NNGH), which is one of the most known commercial inhibitors of MMPs, is described for the first time.

Details

ISSN :
00222836
Volume :
336
Database :
OpenAIRE
Journal :
Journal of Molecular Biology
Accession number :
edsair.doi.dedup.....13b13f25c7b2b583afe3b5c866d49fc8
Full Text :
https://doi.org/10.1016/j.jmb.2003.12.033