4r3v
From Proteopedia
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| - | ''' | + | ==Structure of karilysin propeptide and catalytic MMP domain== |
| - | + | <StructureSection load='4r3v' size='340' side='right' caption='[[4r3v]], [[Resolution|resolution]] 2.01Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4r3v]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R3V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R3V 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xs3|2xs3]], [[2xs4|2xs4]], [[4in9|4in9]]</td></tr> | |
| - | + | <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=4r3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r3v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r3v RCSB], [http://www.ebi.ac.uk/pdbsum/4r3v PDBsum]</span></td></tr> | |
| - | [[Category: | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/KLY_TANFA KLY_TANFA]] Metalloprotease able to cleave casein, gelatin, elastin, fibrinogen and fibronectin. Shows exclusive preference for hydrophobic residues, especially Leu, Tyr and Met, at the P1' position of substrates, and for Pro or Ala at P3. Can efficiently cleave the antimicrobial peptide LL-37 which is a component of the immune system, leading to a significant reduction of its bactericidal activity. Is also able to inhibit all pathways of the human complement system. The classical and lectin complement pathways are inhibited because of the efficient degradation of mannose-binding lectin, ficolin-2, ficolin-3, and C4 by karilysin, whereas inhibition of the terminal pathway is caused by cleavage of C5. Thus, karilysin appears to be a major virulence factor of T.forsythia that contributes to evasion of the human immune response and periodontal disease. Seems to act synergistically with gingipains from the periodontal pathogen P.gingivalis present at the same sites of infection.<ref>PMID:19919176</ref> <ref>PMID:20375548</ref> <ref>PMID:21166898</ref> <ref>PMID:22287711</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Arolas, J L]] | ||
| + | [[Category: Gomis-Ruth, F X]] | ||
| + | [[Category: Guevara, T]] | ||
| + | [[Category: Karim, A Y]] | ||
| + | [[Category: Ksiazek, M]] | ||
[[Category: Lopez-Pelegrin, M]] | [[Category: Lopez-Pelegrin, M]] | ||
[[Category: Potempa, J]] | [[Category: Potempa, J]] | ||
| - | [[Category: | + | [[Category: Bacterial matrix metalloproteinase-like enzyme]] |
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | + | [[Category: Matrix metalloproteinase with unique propeptide]] | |
| - | [[Category: | + | [[Category: Metzincin metallopeptidase]] |
| - | [[Category: | + | |
Revision as of 16:18, 7 January 2015
Structure of karilysin propeptide and catalytic MMP domain
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