1rm8: Difference between revisions
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[[Image:1rm8.gif|left|200px]] | [[Image:1rm8.gif|left|200px]] | ||
'''Crystal structure of the catalytic domain of MMP-16/MT3-MMP: Characterization of MT-MMP specific features''' | {{Structure | ||
|PDB= 1rm8 |SIZE=350|CAPTION= <scene name='initialview01'>1rm8</scene>, resolution 1.80Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=BAT:4-(N-HYDROXYAMINO)-2R-ISOBUTYL-2S-(2-THIENYLTHIOMETHYL)SUCCINYL-L-PHENYLALANINE-N-METHYLAMIDE'>BAT</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of the catalytic domain of MMP-16/MT3-MMP: Characterization of MT-MMP specific features''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1RM8 is a [ | 1RM8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RM8 OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of the catalytic domain of MMP-16/MT3-MMP: characterization of MT-MMP specific features., Lang R, Braun M, Sounni NE, Noel A, Frankenne F, Foidart JM, Bode W, Maskos K, J Mol Biol. 2004 Feb 6;336(1):213-25. PMID:[http:// | Crystal structure of the catalytic domain of MMP-16/MT3-MMP: characterization of MT-MMP specific features., Lang R, Braun M, Sounni NE, Noel A, Frankenne F, Foidart JM, Bode W, Maskos K, J Mol Biol. 2004 Feb 6;336(1):213-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14741217 14741217] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: protease]] | [[Category: protease]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:53:30 2008'' | ||
Revision as of 11:53, 20 March 2008
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| 1rm8, resolution 1.80Å | |||||||||||||
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| Ligands: | ZN, CA and BAT | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal structure of the catalytic domain of MMP-16/MT3-MMP: Characterization of MT-MMP specific features
Overview
Membrane-type matrix metalloproteinases (MT-MMPs) have attracted strong attention, because four of them can activate a key player in the tumor scenario, proMMP-2/progelatinase A. In addition to this indirect effect on the cellular environment, these MT-MMPs degrade extracellular matrix proteins, and their overproduction is associated with tumor growth. We have solved the structure of the catalytic domain (cd) of MT3-MMP/MMP-16 in complex with the hydroxamic acid inhibitor batimastat. CdMT3-MMP exhibits a classical MMP-fold with similarity to MT1-MMP. Nevertheless, it also shows unique properties such as a modified MT-specific loop and a closed S1' specificity pocket, which might help to design specific inhibitors. Some MT-MMP-specific features, derived from the crystal structures of MT-1-MMP determined previously and MT3-MMP, and revealed in recent mutagenesis experiments, explain the impaired interaction of the MT-MMPs with TIMP-1. Docking experiments with proMMP-2 show some exposed loops including the MT-loop of cdMT3-MMP involved in the interaction with the proMMP-2 prodomain in the activation encounter complex. This model might help to understand the experimentally proven importance of the MT-loop for the activation of proMMP-2.
About this Structure
1RM8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the catalytic domain of MMP-16/MT3-MMP: characterization of MT-MMP specific features., Lang R, Braun M, Sounni NE, Noel A, Frankenne F, Foidart JM, Bode W, Maskos K, J Mol Biol. 2004 Feb 6;336(1):213-25. PMID:14741217
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