5ue2: Difference between revisions
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==proMMP-7 with heparin octasaccharide bridging between domains== | ==proMMP-7 with heparin octasaccharide bridging between domains== | ||
<StructureSection load='5ue2' size='340' side='right'caption='[[5ue2 | <StructureSection load='5ue2' size='340' side='right'caption='[[5ue2]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ue2]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5ue2]] 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=5UE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UE2 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=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><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> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ue2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ue2 OCA], [https://pdbe.org/5ue2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ue2 RCSB], [https://www.ebi.ac.uk/pdbsum/5ue2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ue2 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Fulcher YG]] | |||
[[Category: Linhardt RJ]] | |||
[[Category: Fulcher | [[Category: Prior SH]] | ||
[[Category: Linhardt | [[Category: Van Doren SR]] | ||
[[Category: Prior | |||
[[Category: | |||
Revision as of 13:25, 14 June 2023
proMMP-7 with heparin octasaccharide bridging between domainsproMMP-7 with heparin octasaccharide bridging between domains
Structural highlights
FunctionMMP7_HUMAN Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase.[1] Publication Abstract from PubMedHeparan 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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