3ba0

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{{Seed}}
 
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[[Image:3ba0.png|left|200px]]
 
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==Crystal structure of full-length human MMP-12==
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The line below this paragraph, containing "STRUCTURE_3ba0", creates the "Structure Box" on the page.
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<StructureSection load='3ba0' size='340' side='right'caption='[[3ba0]], [[Resolution|resolution]] 3.00&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'>[[3ba0]] 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=3BA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BA0 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]] 3&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HAE:ACETOHYDROXAMIC+ACID'>HAE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_3ba0| PDB=3ba0 | 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=3ba0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ba0 OCA], [https://pdbe.org/3ba0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ba0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ba0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ba0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MMP12_HUMAN MMP12_HUMAN] May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.
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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/ba/3ba0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3ba0 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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The proteolytic activity of matrix metalloproteinases toward extracellular matrix components (ECM), cytokines, chemokines, and membrane receptors is crucial for several homeostatic and pathological processes. Active MMPs are a family of single-chain enzymes (23 family members in the human genome), most of which constituted by a catalytic domain and by a hemopexin-like domain connected by a linker. The X-ray structures of MMP-1 and MMP-2 suggest a conserved and well-defined spatial relationship between the two domains. Here we present structural data for MMP-12, suitably stabilized against self-hydrolysis, both in solution (NMR and SAXS) and in the solid state (X-ray), showing that the hemopexin-like and the catalytic domains experience conformational freedom with respect to each other on a time scale shorter than 10 (-8) s. Hints on the probable conformations are also obtained. This experimental finding opens new perspectives for the often hypothesized active role of the hemopexin-like domain in the enzymatic activity of MMPs.
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===Crystal structure of full-length human MMP-12===
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Evidence of Reciprocal Reorientation of the Catalytic and Hemopexin-Like Domains of Full-Length MMP-12.,Bertini I, Calderone V, Fragai M, Jaiswal R, Luchinat C, Melikian M, Mylonas E, Svergun DI J Am Chem Soc. 2008 May 9;. PMID:18465858<ref>PMID:18465858</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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</div>
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<div class="pdbe-citations 3ba0" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18465858}}, adds the Publication Abstract to the page
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*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18465858 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18465858}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3BA0 is a 1 chain 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=3BA0 OCA].
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==Reference==
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<ref group="xtra">PMID:18465858</ref><ref group="xtra">PMID:15611040</ref><ref group="xtra">PMID:12032297</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Macrophage elastase]]
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[[Category: Large Structures]]
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[[Category: Bertini, I.]]
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[[Category: Bertini I]]
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[[Category: Calderone, V.]]
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[[Category: Calderone V]]
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[[Category: Fragai, M.]]
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[[Category: Fragai M]]
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[[Category: Jaiswal, R.]]
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[[Category: Jaiswal R]]
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[[Category: Luchinat, C.]]
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[[Category: Luchinat C]]
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[[Category: Melikian, M.]]
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[[Category: Melikian M]]
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[[Category: Myonas, E.]]
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[[Category: Myonas E]]
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[[Category: Svergun, D I.]]
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[[Category: Svergun DI]]
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[[Category: Calcium]]
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[[Category: Catalytic domain]]
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[[Category: Domain interaction.]]
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[[Category: Extracellular matrix]]
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[[Category: Full-length mmp-12]]
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[[Category: Glycoprotein]]
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[[Category: Hemopexin domain]]
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[[Category: Hydrolase]]
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[[Category: Metal-binding]]
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[[Category: Metalloprotease]]
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[[Category: Polymorphism]]
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[[Category: Protease]]
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[[Category: Secreted]]
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[[Category: Zinc]]
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[[Category: Zymogen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 22:03:00 2009''
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Current revision

Crystal structure of full-length human MMP-12

PDB ID 3ba0

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