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|Title:||Crystal structure of the catalytic domain of human matrix metalloproteinase 10||Authors:||I., Bertini
|Keywords:||matrix metalloproteinase, stromelysin-2, MMP-10, crystal structure, inhibitor||Issue Date:||2004||Project:||None||Journal:||JOURNAL OF MOLECULAR BIOLOGY||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.
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