Structural highlights
1q3a is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , |
| Related: | 1g49, 1bqo, 1d5j, 1d8f, 1uea |
| Gene: | MMP10 OR STMY2 (HUMAN) |
| Activity: | Stromelysin 2, with EC number 3.4.24.22 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[MMP10_HUMAN] Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bertini I, Calderone V, Fragai M, Luchinat C, Mangani S, Terni B. Crystal structure of the catalytic domain of human matrix metalloproteinase 10. J Mol Biol. 2004 Feb 20;336(3):707-16. PMID:15095982 doi:10.1016/j.jmb.2003.12.033
