3m1h
From Proteopedia
(Difference between revisions)
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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=3m1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m1h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m1h RCSB], [http://www.ebi.ac.uk/pdbsum/3m1h PDBsum]</span></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=3m1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m1h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m1h RCSB], [http://www.ebi.ac.uk/pdbsum/3m1h PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/KGP83_PORGN KGP83_PORGN]] Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria (By similarity).[UniProtKB:B2RLK2] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 21:38, 25 December 2014
Crystal Structure Analysis of the K3 Cleaved Adhesin Domain of Lys-gingipain (Kgp) from Porphyromonas gingivalis w83
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