1mmp: Difference between revisions

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-[[Image:1mmp.jpg|left|200px]]<br /><applet load="1mmp" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1mmp, resolution 2.3&Aring;" />
-'''MATRILYSIN COMPLEXED WITH CARBOXYLATE INHIBITOR'''<br />
-==Overview==
+==MATRILYSIN COMPLEXED WITH CARBOXYLATE INHIBITOR==
-Matrix metalloproteases are a family of enzymes that play critical roles, in the physiological and pathological degradation of the extracellular, matrix. These enzymes may be important therapeutic targets for the, treatment of various diseases where tissue degradation is part of the, pathology, such as cancer and arthritis. Matrilysin is the smallest member, of this family of enzymes, all of which require zinc for catalytic, activity. The first X-ray crystal structures of human matrilysin are, presented. Inhibitors of metalloproteases are often characterized by the, chemical group that interacts with the active site zinc of the protein., The structures of matrilysin complexed with hydroxamate (maximum, resolution 1.9 A), carboxylate (maximum resolution 2.4 A), and, sulfodiimine (maximum resolution 2.3 A) inhibitors are presented here and, provide detailed information about how each functional group interacts, with the catalytic zinc. Only the zinc-coordination group is variable in, this series of inhibitors. Examination of these inhibitor-matrilysin, complexes emphasizes the dominant role the zinc-coordinating group plays, in determining the relative potencies of the inhibitors. The structures of, these matrilysin-inhibitor complexes also provide a basis for comparing, the catalytic mechanism of MMPs and other metalloproteins.
+<StructureSection load='1mmp' size='340' side='right'caption='[[1mmp]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1mmp]] is a 2 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=1MMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MMP FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=RSS:5-METHYL-3-(9-OXO-1,8-DIAZA-TRICYCLO[10.6.1.013,18]NONADECA-12(19),13,15,17-TETRAEN-10-YLCARBAMOYL)-HEXANOIC+ACID'>RSS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mmp OCA], [https://pdbe.org/1mmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mmp RCSB], [https://www.ebi.ac.uk/pdbsum/1mmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mmp ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MMP7_HUMAN MMP7_HUMAN] Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase.<ref>PMID:2550050</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mm/1mmp_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1mmp ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-MMP 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 <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=RSS:'>RSS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Matrilysin Matrilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.23 3.4.24.23] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MMP OCA].
+*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
+== References ==
-==Reference==
+<references/>
-Matrilysin-inhibitor complexes: common themes among metalloproteases., Browner MF, Smith WW, Castelhano AL, Biochemistry. 1995 May 23;34(20):6602-10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7756291 7756291]
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Matrilysin]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Browner MF]]
-[[Category: Browner, M.F.]]
+[[Category: Castelhano AL]]
-[[Category: Castelhano, A.L.]]
+[[Category: Smith WW]]
-[[Category: Smith, W.W.]]
-[[Category: CA]]
-[[Category: RSS]]
-[[Category: ZN]]
-[[Category: metalloprotease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:24:55 2008''