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1q3a
From Proteopedia
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(New page: 200px<br /> <applet load="1q3a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q3a, resolution 2.10Å" /> '''Crystal structure o...)
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Revision as of 16:43, 12 November 2007
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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
Page seeded by OCA on Mon Nov 12 18:50:01 2007
Categories: Homo sapiens | Single protein | Stromelysin 2 | Bertini, I. | Calderone, V. | Fragai, M. | Luchinat, C. | Mangani, S. | Terni, B. | CA | NGH | ZN | Hydroxamic acid | Inhibitors | Metalloproteinase | Mmp-10 | Nngh | Stromelysin-2
