5ue5

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==proMMP-7 with heparin octasaccharide bound to the catalytic domain==
==proMMP-7 with heparin octasaccharide bound to the catalytic domain==
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<StructureSection load='5ue5' size='340' side='right' caption='[[5ue5]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''>
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<StructureSection load='5ue5' size='340' side='right'caption='[[5ue5]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ue5]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UE5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UE5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ue5]] 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=5UE5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UE5 FirstGlance]. <br>
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</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=IDS:2-O-SULFO-ALPHA-L-IDOPYRANURONIC+ACID'>IDS</scene>, <scene name='pdbligand=SGN:N,O6-DISULFO-GLUCOSAMINE'>SGN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mze|2mze]], [[5ue2|5ue2]]</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=IDS:2-O-SULFO-ALPHA-L-IDOPYRANURONIC+ACID'>IDS</scene>, <scene name='pdbligand=SGN:N,O6-DISULFO-GLUCOSAMINE'>SGN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<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'>[https://proteopedia.org/fgij/fg.htm?mol=5ue5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ue5 OCA], [https://pdbe.org/5ue5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ue5 RCSB], [https://www.ebi.ac.uk/pdbsum/5ue5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ue5 ProSAT]</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=5ue5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ue5 OCA], [http://pdbe.org/5ue5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ue5 RCSB], [http://www.ebi.ac.uk/pdbsum/5ue5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ue5 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Heparan sulfate proteoglycans activate the matrix metalloproteinase-7 zymogen (proMMP-7) and recruit it in order to shed proteins from cell surfaces. This occurs in uterine and mammary epithelia, bacterial killing, lung healing, and tumor cell signaling. Basic tracks on proMMP-7 recognize polyanionic heparin, according to nuclear magnetic resonance and mutations disruptive of maturation. Contacts and proximity measurements guided docking of a heparin octasaccharide to proMMP-7. The reducing end fits into a basic pocket in the pro-domain while the chain continues toward the catalytic domain. Another oligosaccharide traverses a basic swath remote on the catalytic domain and inserts its reducing end into a slot formed with the basic C terminus. This latter association appears to support allosteric acceleration of proteolysis. The modes of binding account for extended, heterogeneous assemblies of proMMP-7 with heparinoids during maturation and for bridging to pro-alpha-defensins and proteoglycans. These associations support proteolytic release of activities at epithelial cell surfaces.
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Glycan Activation of a Sheddase: Electrostatic Recognition between Heparin and proMMP-7.,Fulcher YG, Prior SH, Masuko S, Li L, Pu D, Zhang F, Linhardt RJ, Van Doren SR Structure. 2017 Jul 5;25(7):1100-1110.e5. doi: 10.1016/j.str.2017.05.019. Epub, 2017 Jun 22. PMID:28648610<ref>PMID:28648610</ref>
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==See Also==
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*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
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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 5ue5" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Matrilysin]]
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[[Category: Homo sapiens]]
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[[Category: Doren, S R.Van]]
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[[Category: Large Structures]]
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[[Category: Fulcher, Y G]]
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[[Category: Fulcher YG]]
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[[Category: Linhardt, R J]]
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[[Category: Linhardt RJ]]
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[[Category: Prior, S H]]
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[[Category: Prior SH]]
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[[Category: Allosteric effector site]]
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[[Category: Van Doren SR]]
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[[Category: Enzyme complex with heparin oligosaccharide]]
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[[Category: Glycan complex with protein]]
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[[Category: Hydrolase]]
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[[Category: Zymogen]]
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Current revision

proMMP-7 with heparin octasaccharide bound to the catalytic domain

PDB ID 5ue5

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