1rm8
From Proteopedia
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|PDB= 1rm8 |SIZE=350|CAPTION= <scene name='initialview01'>1rm8</scene>, resolution 1.80Å | |PDB= 1rm8 |SIZE=350|CAPTION= <scene name='initialview01'>1rm8</scene>, resolution 1.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BAT:4-(N-HYDROXYAMINO)-2R-ISOBUTYL-2S-(2-THIENYLTHIOMETHYL)SUCCINYL-L-PHENYLALANINE-N-METHYLAMIDE'>BAT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1bqq|1BQQ]], [[1jk3|1JK3]], [[1mmb|1MMB]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rm8 OCA], [http://www.ebi.ac.uk/pdbsum/1rm8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rm8 RCSB]</span> | ||
}} | }} | ||
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[[Category: Noel, A]] | [[Category: Noel, A]] | ||
[[Category: Sounni, N E.]] | [[Category: Sounni, N E.]] | ||
| - | [[Category: BAT]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: ZN]] | ||
[[Category: batimastat]] | [[Category: batimastat]] | ||
[[Category: hydroxamate inhibitor]] | [[Category: hydroxamate inhibitor]] | ||
| Line 41: | Line 41: | ||
[[Category: protease]] | [[Category: protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:30:06 2008'' |
Revision as of 20:30, 30 March 2008
| |||||||
| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1BQQ, 1JK3, 1MMB
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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