1rm8

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[[Image:1rm8.png|left|200px]]
 
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==Crystal structure of the catalytic domain of MMP-16/MT3-MMP: Characterization of MT-MMP specific features==
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The line below this paragraph, containing "STRUCTURE_1rm8", creates the "Structure Box" on the page.
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<StructureSection load='1rm8' size='340' side='right'caption='[[1rm8]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1rm8]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RM8 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
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{{STRUCTURE_1rm8| PDB=1rm8 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rm8 OCA], [https://pdbe.org/1rm8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rm8 RCSB], [https://www.ebi.ac.uk/pdbsum/1rm8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rm8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MMP16_HUMAN MMP16_HUMAN] Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rm/1rm8_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rm8 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Crystal structure of the catalytic domain of MMP-16/MT3-MMP: Characterization of MT-MMP specific features===
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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<ref>PMID:14741217</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_14741217}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1rm8" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 14741217 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14741217}}
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==About this Structure==
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[[1rm8]] is a 1 chain structure of [[Elastase]] with 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].
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==See Also==
==See Also==
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*[[Elastase]]
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*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:14741217</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Bode, W.]]
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[[Category: Large Structures]]
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[[Category: Braun, M.]]
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[[Category: Bode W]]
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[[Category: Foidart, J M.]]
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[[Category: Braun M]]
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[[Category: Frankenne, F.]]
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[[Category: Foidart J-M]]
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[[Category: Lang, R.]]
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[[Category: Frankenne F]]
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[[Category: Maskos, K.]]
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[[Category: Lang R]]
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[[Category: Noel, A]]
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[[Category: Maskos K]]
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[[Category: Sounni, N E.]]
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[[Category: Noel A]]
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[[Category: Batimastat]]
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[[Category: Sounni NE]]
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[[Category: Hydrolase]]
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[[Category: Hydroxamate inhibitor]]
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[[Category: Membrane type - matrix metalloproteinase]]
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[[Category: Mmp-16]]
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[[Category: Mt-mmp]]
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[[Category: Mt3-mmp]]
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[[Category: Protease]]
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Current revision

Crystal structure of the catalytic domain of MMP-16/MT3-MMP: Characterization of MT-MMP specific features

PDB ID 1rm8

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