Helicobacter pylori CagA Inhibits PAR1/MARK Family Kinases by Mimicking Host Substrates

The CagA protein of Helicobacter pylori interacts with numerous cellular factors, and is associated with increased virulence and risk of gastric carcinoma. We present here the co-crystal structure of a subdomain of CagA with the human kinase PAR1b/MARK2, revealing that a CagA peptide mimics substrat...

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Detalles Bibliográficos
Autores principales: Neišić, Dragana, Miller, Marshall C., Quinkert, Zachary T., Stein, Markus, Chait, Brian T., Stebbins, C. Erec
Formato: Texto
Lenguaje:English
Publicado: 2009
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3006182/
https://www.ncbi.nlm.nih.gov/pubmed/19966800
http://dx.doi.org/10.1038/nsmb.1705
Descripción
Sumario:The CagA protein of Helicobacter pylori interacts with numerous cellular factors, and is associated with increased virulence and risk of gastric carcinoma. We present here the co-crystal structure of a subdomain of CagA with the human kinase PAR1b/MARK2, revealing that a CagA peptide mimics substrates of this kinase family, resembling eukaryotic protein kinase inhibitors. Mutagenesis of conserved residues central to this interaction renders CagA inactive as an inhibitor of MARK2.

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