2clt: Difference between revisions

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-[[Image:2clt.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_2clt", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_2clt|  PDB=2clt  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE ACTIVE FORM (FULL-LENGTH) OF HUMAN FIBROBLAST COLLAGENASE.'''
+==Crystal structure of the active form (full-length) of human fibroblast collagenase.==
+<StructureSection load='2clt' size='340' side='right'caption='[[2clt]], [[Resolution|resolution]] 2.67&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2clt]] 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=2CLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CLT 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]] 2.67&#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=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=2clt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2clt OCA], [https://pdbe.org/2clt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2clt RCSB], [https://www.ebi.ac.uk/pdbsum/2clt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2clt ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MMP1_HUMAN MMP1_HUMAN] Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity.<ref>PMID:1645757</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/cl/2clt_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2clt ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The extracellular matrix is a dynamic environment that constantly undergoes remodelling and degradation during vital physiological processes such as angiogenesis, wound healing, and development. Unbalanced extracellular matrix breakdown is associated with many diseases such as arthritis, cancer and fibrosis. Interstitial collagen is degraded by matrix metalloproteinases with collagenolytic activity by MMP-1, MMP-8 and MMP-13, collectively known as the collagenases. Matrix metalloproteinase 1 (MMP-1) plays a pivotal role in degradation of interstitial collagen types I, II, and III. Here, we report the crystal structure of the active form of human MMP-1 at 2.67 A resolution. This is the first MMP-1 structure that is free of inhibitor and a water molecule essential for peptide hydrolysis is observed coordinated with the active site zinc. Comparing this structure with the human proMMP-1 shows significant structural differences, mainly in the relative orientation of the hemopexin domain, between the pro form and active form of the human enzyme.
-==Overview==
+Crystal structure of an active form of human MMP-1.,Iyer S, Visse R, Nagase H, Acharya KR J Mol Biol. 2006 Sep 8;362(1):78-88. Epub 2006 Aug 4. PMID:16890240<ref>PMID:16890240</ref>
-The extracellular matrix is a dynamic environment that constantly undergoes remodelling and degradation during vital physiological processes such as angiogenesis, wound healing, and development. Unbalanced extracellular matrix breakdown is associated with many diseases such as arthritis, cancer and fibrosis. Interstitial collagen is degraded by matrix metalloproteinases with collagenolytic activity by MMP-1, MMP-8 and MMP-13, collectively known as the collagenases. Matrix metalloproteinase 1 (MMP-1) plays a pivotal role in degradation of interstitial collagen types I, II, and III. Here, we report the crystal structure of the active form of human MMP-1 at 2.67 A resolution. This is the first MMP-1 structure that is free of inhibitor and a water molecule essential for peptide hydrolysis is observed coordinated with the active site zinc. Comparing this structure with the human proMMP-1 shows significant structural differences, mainly in the relative orientation of the hemopexin domain, between the pro form and active form of the human enzyme.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-CLT 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=2CLT OCA].
+</div>
+<div class="pdbe-citations 2clt" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Crystal structure of an active form of human MMP-1., Iyer S, Visse R, Nagase H, Acharya KR, J Mol Biol. 2006 Sep 8;362(1):78-88. Epub 2006 Aug 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16890240 16890240]
+*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Interstitial collagenase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Acharya KR]]
-[[Category: Acharya, K R.]]
+[[Category: Iyer S]]
-[[Category: Iyer, S.]]
+[[Category: Nagase H]]
-[[Category: Nagase, H.]]
+[[Category: Visse R]]
-[[Category: Visse, R.]]
-[[Category: Autocatalytic cleavage]]
-[[Category: Calcium]]
-[[Category: Collagen]]
-[[Category: Collagen degradation]]
-[[Category: Extracellular matrix]]
-[[Category: Fibroblast collagenase]]
-[[Category: Glycoprotein]]
-[[Category: Hydrolase]]
-[[Category: Inhibitor-free]]
-[[Category: Matrix metalloproteinase]]
-[[Category: Metal-binding]]
-[[Category: Metalloprotease]]
-[[Category: Polymorphism]]
-[[Category: Protease]]
-[[Category: Zinc]]
-[[Category: Zymogen]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 22:27:11 2008''