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| - | {{Large structure}}
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| | ==Membrane Bilayer complex with Matrix Metalloproteinase-12 at its Beta-face== | | ==Membrane Bilayer complex with Matrix Metalloproteinase-12 at its Beta-face== |
| - | <StructureSection load='2mls' size='340' side='right' caption='[[2mls]], [[NMR_Ensembles_of_Models | 14 NMR models]]' scene=''> | + | <StructureSection load='2mls' size='340' side='right'caption='[[2mls]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2mls]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MLS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MLS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2mls]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MLS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PX4:1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PX4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2poj|2poj]], [[2mlr|2mlr]]</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=PX4:1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PX4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MMP12, HME ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2mls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mls OCA], [https://pdbe.org/2mls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mls RCSB], [https://www.ebi.ac.uk/pdbsum/2mls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mls ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Macrophage_elastase Macrophage elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.65 3.4.24.65] </span></td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mls OCA], [http://pdbe.org/2mls PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mls RCSB], [http://www.ebi.ac.uk/pdbsum/2mls PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mls ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | {{Large structure}} | |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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. |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Matrix metalloproteinases (MMPs) regulate tissue remodelling, inflammation and disease progression. Some soluble MMPs are inexplicably active near cell surfaces. Here we demonstrate the binding of MMP-12 directly to bilayers and cellular membranes using paramagnetic NMR and fluorescence. Opposing sides of the catalytic domain engage spin-labelled membrane mimics. Loops project from the beta-sheet interface to contact the phospholipid bilayer with basic and hydrophobic residues. The distal membrane interface comprises loops on the other side of the catalytic cleft. Both interfaces mediate MMP-12 association with vesicles and cell membranes. MMP-12 binds plasma membranes and is internalized to hydrophobic perinuclear features, the nuclear membrane and inside the nucleus within minutes. While binding of TIMP-2 to MMP-12 hinders membrane interactions beside the active site, TIMP-2-inhibited MMP-12 binds vesicles and cells, suggesting compensatory rotation of its membrane approaches. MMP-12 association with diverse cell membranes may target its activities to modulate innate immune responses and inflammation.
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| - | Ambidextrous binding of cell and membrane bilayers by soluble matrix metalloproteinase-12.,Koppisetti RK, Fulcher YG, Jurkevich A, Prior SH, Xu J, Lenoir M, Overduin M, Van Doren SR Nat Commun. 2014 Nov 21;5:5552. doi: 10.1038/ncomms6552. PMID:25412686<ref>PMID:25412686</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 2mls" style="background-color:#fffaf0;"></div>
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| | ==See Also== | | ==See Also== |
| - | *[[Matrix metalloproteinase|Matrix metalloproteinase]] | + | *[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]] |
| - | == References ==
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| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Macrophage elastase]] | + | [[Category: Large Structures]] |
| - | [[Category: Doren, S R.Van]]
| + | [[Category: Fulcher YG]] |
| - | [[Category: Fulcher, Y G]] | + | [[Category: Koppisetti RK]] |
| - | [[Category: Koppisetti, R K]] | + | [[Category: Lenoir M]] |
| - | [[Category: Lenoir, M]] | + | [[Category: Overduin M]] |
| - | [[Category: Overduin, M]] | + | [[Category: Prior SH]] |
| - | [[Category: Prior, S H]] | + | [[Category: Van Doren SR]] |
| - | [[Category: Catalytic domain]] | + | |
| - | [[Category: Hydrolase]]
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| - | [[Category: Membrane-binding of soluble metalloproteinase mmp-12]]
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