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2jxy
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:2jxy.png|left|200px]] | ||
| - | < | + | ==Solution structure of the hemopexin-like domain of MMP12== |
| - | + | <StructureSection load='2jxy' size='340' side='right'caption='[[2jxy]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[2jxy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JXY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JXY FirstGlance]. <br> | |
| - | + | </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></td></tr> | |
| - | - | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Macrophage_elastase Macrophage elastase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.65 3.4.24.65] </span></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=2jxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jxy OCA], [https://pdbe.org/2jxy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jxy RCSB], [https://www.ebi.ac.uk/pdbsum/2jxy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jxy ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [[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. | ||
| + | == 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/jx/2jxy_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=2jxy ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2jxy" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Human]] |
| - | + | [[Category: Large Structures]] | |
| - | + | ||
| - | == | + | |
| - | + | ||
| - | [[Category: | + | |
[[Category: Macrophage elastase]] | [[Category: Macrophage elastase]] | ||
| - | + | [[Category: Bertini, I]] | |
| - | [[Category: Bertini, I | + | [[Category: Calderone, V]] |
| - | [[Category: Calderone, V | + | [[Category: Fragai, M]] |
| - | [[Category: Fragai, M | + | [[Category: Jaiswal, R]] |
| - | [[Category: Jaiswal, R | + | [[Category: Luchinat, C]] |
| - | [[Category: Luchinat, C | + | [[Category: Melikian, M]] |
| - | [[Category: Melikian, M | + | |
[[Category: B-sheet hydrophobic core]] | [[Category: B-sheet hydrophobic core]] | ||
[[Category: Calcium]] | [[Category: Calcium]] | ||
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[[Category: Zinc]] | [[Category: Zinc]] | ||
[[Category: Zymogen]] | [[Category: Zymogen]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:28:00 2008'' | ||
Current revision
Solution structure of the hemopexin-like domain of MMP12
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Categories: Human | Large Structures | Macrophage elastase | Bertini, I | Calderone, V | Fragai, M | Jaiswal, R | Luchinat, C | Melikian, M | B-sheet hydrophobic core | Calcium | Extracellular matrix | Glycoprotein | Hydrolase | Metal-binding | Metalloprotease | Polymorphism | Protease | Secreted | Zinc | Zymogen

