| Literature DB >> 15095982 |
I Bertini1, V Calderone, M Fragai, C Luchinat, S Mangani, B Terni.
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.Entities:
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Year: 2004 PMID： 15095982 DOI： 10.1016/j.jmb.2003.12.033
Source DB: PubMed Journal: J Mol Biol ISSN： 0022-2836 Impact factor: 5.469