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| - | {{Large structure}}
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| | ==NMR Solution Structure of the PRO Form of Human Matrilysin (proMMP-7) in Complex with Zwitterionic Membrane== | | ==NMR Solution Structure of the PRO Form of Human Matrilysin (proMMP-7) in Complex with Zwitterionic Membrane== |
| - | <StructureSection load='2mzh' size='340' side='right' caption='[[2mzh]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2mzh' size='340' side='right'caption='[[2mzh]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2mzh]] 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=2MZH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MZH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2mzh]] 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=2MZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MZH 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">[[2mze|2mze]], [[2mzi|2mzi]]</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">MMP7, MPSL1, PUMP1 ([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=2mzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mzh OCA], [https://pdbe.org/2mzh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mzh RCSB], [https://www.ebi.ac.uk/pdbsum/2mzh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mzh 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/Matrilysin Matrilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.23 3.4.24.23] </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=2mzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mzh OCA], [http://pdbe.org/2mzh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mzh RCSB], [http://www.ebi.ac.uk/pdbsum/2mzh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mzh ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | {{Large structure}} | |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Matrix metalloproteinase|Matrix metalloproteinase]] | + | *[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Matrilysin]] | + | [[Category: Large Structures]] |
| - | [[Category: Doren, S R.Van]]
| + | [[Category: Prior SH]] |
| - | [[Category: Prior, S H]] | + | [[Category: Van Doren SR]] |
| - | [[Category: Hydrolase]] | + | |
| - | [[Category: Metalloenzyme]]
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| - | [[Category: Zwitterionic membrane-bound form]]
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| - | [[Category: Zymogen]]
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| Structural highlights
Function
MMP7_HUMAN Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase.[1]
Publication Abstract from PubMed
Matrix metalloproteinase-7 (MMP-7) sheds signaling proteins from cell surfaces to activate bacterial killing, wound healing, and tumorigenesis. The mechanism targeting soluble MMP-7 to membranes has been investigated. Nuclear magnetic resonance structures of the zymogen, free and bound to membrane mimics without and with anionic lipid, reveal peripheral binding to bilayers through paramagnetic relaxation enhancements. Addition of cholesterol sulfate partially embeds the protease in the bilayer, restricts its diffusion, and tips the active site away from the bilayer. Its insertion of hydrophobic residues organizes the lipids, pushing the head groups and sterol sulfate outward toward the enzyme's positive charge on the periphery of the enlarged interface. Fluorescence probing demonstrates a similar mode of binding to plasma membranes and internalized vesicles of colon cancer cells. Binding of bilayered micelles induces allosteric activation and conformational change in the auto-inhibitory peptide and the adjacent scissile site, illustrating a potential intermediate in the activation of the zymogen.
Charge-Triggered Membrane Insertion of Matrix Metalloproteinase-7, Supporter of Innate Immunity and Tumors.,Prior SH, Fulcher YG, Koppisetti RK, Jurkevich A, Van Doren SR Structure. 2015 Nov 3;23(11):2099-110. doi: 10.1016/j.str.2015.08.013. Epub 2015 , Oct 1. PMID:26439767[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Quantin B, Murphy G, Breathnach R. Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members. Biochemistry. 1989 Jun 27;28(13):5327-34. PMID:2550050
- ↑ Prior SH, Fulcher YG, Koppisetti RK, Jurkevich A, Van Doren SR. Charge-Triggered Membrane Insertion of Matrix Metalloproteinase-7, Supporter of Innate Immunity and Tumors. Structure. 2015 Nov 3;23(11):2099-110. doi: 10.1016/j.str.2015.08.013. Epub 2015 , Oct 1. PMID:26439767 doi:http://dx.doi.org/10.1016/j.str.2015.08.013
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