1q3a: Difference between revisions
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==Overview== | ==Overview== | ||
The catalytic domain of matrix metalloproteinase-10 (MMP-10) has been | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: stromelysin-2]] | [[Category: stromelysin-2]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:35:26 2008'' | ||
Revision as of 12:35, 21 February 2008
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Crystal structure of the catalytic domain of human matrix metalloproteinase 10
Overview
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.
About this Structure
1Q3A is a Single protein structure of sequence from Homo sapiens with ZN, CA and NGH as ligands. Active as Stromelysin 2, with EC number 3.4.24.22 Full crystallographic information is available from OCA.
Reference
Crystal structure of the catalytic domain of human matrix metalloproteinase 10., Bertini I, Calderone V, Fragai M, Luchinat C, Mangani S, Terni B, J Mol Biol. 2004 Feb 20;336(3):707-16. PMID:15095982
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