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Crystal structure of the catalytic domain of human matrix metalloproteinase 10.

Bertini I., Calderone V., Fragai M., Luchinat C., Mangani S., Terni B.

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.

J. Mol. Biol. 336:707-716(2004) [PubMed] [Europe PMC]

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