3IEC

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

Summary for 3IEC

• Entry DOI: 10.2210/pdb3iec/pdb
• Descriptor: Serine/threonine-protein kinase MARK2, Cytotoxicity-associated immunodominant antigen (3 entities in total)
• Functional Keywords: protein-protein complex, kinase, virulence factor, alternative promoter usage, atp-binding, cell membrane, developmental protein, differentiation, magnesium, membrane, metal-binding, nucleotide-binding, phosphoprotein, serine/threonine-protein kinase, transferase, signaling protein-toxin complex, signaling protein/toxin
• Biological source: Homo sapiens (human); More
• Cellular location: Cell membrane; Peripheral membrane protein: Q7KZI7
• Total number of polymer chains: 8
• Total formula weight: 201371.44

Authors

Stebbins, C.E.,Nesic, D.,Miller, M. (deposition date: 2009-07-22, release date: 2009-12-08, Last modification date: 2024-02-21)

Primary citation

Nesic, D.,Miller, M.C.,Quinkert, Z.T.,Stein, M.,Chait, B.T.,Stebbins, C.E.
Helicobacter pylori CagA inhibits PAR1-MARK family kinases by mimicking host substrates.
Nat.Struct.Mol.Biol., 17:130-132, 2010

PubMed Abstract: 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 cocrystal 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.

PubMed: 19966800
DOI: 10.1038/nsmb.1705

Experimental method

X-RAY DIFFRACTION (2.2 Å)