1sln

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[[Image:1sln.gif|left|200px]]<br />
 
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<applet load="1sln" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1sln, resolution 2.27&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THE N-CARBOXY-ALKYL INHIBITOR L-702,842'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THE N-CARBOXY-ALKYL INHIBITOR L-702,842==
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The proteolytic enzyme stromelysin-1 is a member of the family of matrix, metalloproteinases and is believed to play a role in pathological, conditions such as arthritis and tumor invasion. Stromelysin-1 is, synthesized as a pro-enzyme that is activated by removal of an N-terminal, prodomain. The active enzyme contains a catalytic domain and a C-terminal, hemopexin domain believed to participate in macromolecular substrate, recognition. We have determined the three-dimensional structures of both a, C-truncated form of the proenzyme and an inhibited complex of the, catalytic domain by X-ray diffraction analysis. The catalytic core is very, similar in the two forms and is similar to the homologous domain in, fibroblast and neutrophil collagenases, as well as to the stromelysin, structure ... [[http://ispc.weizmann.ac.il/pmbin/getpm?8535233 (full description)]]
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<StructureSection load='1sln' size='340' side='right'caption='[[1sln]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1sln]] 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=1SLN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SLN FirstGlance]. <br>
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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]] 2.27&#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=8MI:N-(R-CARBOXY-ETHYL)-ALPHA-(S)-(2-PHENYLETHYL)GLYCYL-L-ARGININE-N-PHENYLAMIDE'>8MI</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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=1sln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sln OCA], [https://pdbe.org/1sln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sln RCSB], [https://www.ebi.ac.uk/pdbsum/1sln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sln ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/MMP3_HUMAN MMP3_HUMAN] Defects in MMP3 are the cause of susceptibility to coronary heart disease type 6 (CHDS6) [MIM:[https://omim.org/entry/614466 614466]. A multifactorial disease characterized by an imbalance between myocardial functional requirements and the capacity of the coronary vessels to supply sufficient blood flow. Decreased capacity of the coronary vessels is often associated with thickening and loss of elasticity of the coronary arteries. Note=A polymorphism in the MMP3 promoter region is associated with the risk of coronary heart disease and myocardial infarction, due to lower MMP3 proteolytic activity and higher extracellular matrix deposition in atherosclerotic lesions.<ref>PMID:8662692</ref> <ref>PMID:12477941</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/MMP3_HUMAN MMP3_HUMAN] Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase.
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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/sl/1sln_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=1sln ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1SLN is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with ZN, CA and INH as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Hydrolase Hydrolase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.17 3.4.24.17]]. Structure known Active Sites: CA1, CA2, CA3, INH, ZN1 and ZN2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SLN OCA]].
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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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Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme., Becker JW, Marcy AI, Rokosz LL, Axel MG, Burbaum JJ, Fitzgerald PM, Cameron PM, Esser CK, Hagmann WK, Hermes JD, et al., Protein Sci. 1995 Oct;4(10):1966-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8535233 8535233]
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Becker, J.W.]]
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[[Category: Becker JW]]
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[[Category: CA]]
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[[Category: INH]]
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[[Category: ZN]]
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[[Category: collagen degradation]]
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[[Category: fibroblast]]
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[[Category: hydrolase]]
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[[Category: metalloprotease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:42:46 2007''
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Current revision

CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THE N-CARBOXY-ALKYL INHIBITOR L-702,842

PDB ID 1sln

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