3km5

Crystal Structure Analysis of the K2 Cleaved Adhesin Domain of Lys-gingipain (Kgp)Crystal Structure Analysis of the K2 Cleaved Adhesin Domain of Lys-gingipain (Kgp)

Template:ABSTRACT PUBMED 20233299

FunctionFunction

[O52050_PORGI] 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]

About this StructureAbout this Structure

3km5 is a 2 chain structure with sequence from Porphyromonas gingivalis. Full crystallographic information is available from OCA.

ReferenceReference

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↑ Li N, Yun P, Nadkarni MA, Ghadikolaee NB, Nguyen KA, Lee M, Hunter N, Collyer CA. Structure determination and analysis of a haemolytic gingipain adhesin domain from Porphyromonas gingivalis. Mol Microbiol. 2010 May;76(4):861-73. Epub 2010 Mar 10. PMID:20233299 doi:10.1111/j.1365-2958.2010.07123.x

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OCA

[1] Li N, Yun P, Nadkarni MA, Ghadikolaee NB, Nguyen KA, Lee M, Hunter N, Collyer CA. Structure determination and analysis of a haemolytic gingipain adhesin domain from Porphyromonas gingivalis. Mol Microbiol. 2010 May;76(4):861-73. Epub 2010 Mar 10. PMID:20233299 doi:10.1111/j.1365-2958.2010.07123.x

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