ArticleProtein science : a publication of the Protein Society2015
Structure of the lysine specific protease Kgp from Porphyromonas gingivalis, a target for improved oral health.
Article in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Discovery of Gingipains andFoods (Basel, Switzerland) · 2025Review
- Structural and functional studies of legumain-mycocypin complexes revealed a competitive, exosite-regulated mode of interaction.The Journal of biological chemistry · 2022Article
- Intermolecular latency regulates the essential C-terminal signal peptidase and sortase of theProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Existence of natural mouse IgG mAbs recognising epitopes shared by malondialdehyde acetaldehyde adducts andInnate immunity · 2021Article
- Structures of the free and inhibitors-bound forms of bromelain and ananain from Ananas comosus stem and in vitro study of their cytotoxicity.Scientific reports · 2020Article
- Pathogenesis of Important Virulence Factors ofFrontiers in cellular and infection microbiology · 2019Review
- Article
- Crystal Structure and Activity Studies of the C11 Cysteine Peptidase from Parabacteroides merdae in the Human Gut Microbiome.The Journal of biological chemistry · 2016Article
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Authors and funding
8 authors.
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Abstract
The oral pathogen Porphyromonas gingivalis is a keystone pathogen in the development of chronic periodontitis. Gingipains, the principle virulence factors of P. gingivalis are multidomain, cell-surface proteins containing a cysteine protease domain. The lysine specific gingipain, Kgp, is a critical virulence factor of P. gingivalis. We have determined the X-ray crystal structure of the lysine-specific protease domain of Kgp to 1.6 Å resolution. The structure provides insights into the mechanism of substrate specificity and catalysis.
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