3m1h
From Proteopedia
Contents |
Crystal Structure Analysis of the K3 Cleaved Adhesin Domain of Lys-gingipain (Kgp) from Porphyromonas gingivalis w83
Template:ABSTRACT PUBMED 21812842
Function
[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]
About this Structure
3m1h is a 4 chain structure with sequence from Porphyromonas gingivalis w83. Full crystallographic information is available from OCA.
Reference
- Li N, Yun P, Jeffries CM, Langley D, Gamsjaeger R, Church WB, Hunter N, Collyer CA. The modular structure of haemagglutinin/adhesin regions in gingipains of Porphyromonas gingivalis. Mol Microbiol. 2011 Sep;81(5):1358-73. doi: 10.1111/j.1365-2958.2011.07768.x., Epub 2011 Aug 4. PMID:21812842 doi:10.1111/j.1365-2958.2011.07768.x
