Listeria InlB takes a different route to met.
InlB, a surface protein of the human bacterial pathogen Listeria monocytogenes, interacts with the receptor tyrosine kinase Met on host cells to enable bacterial invasion. In this issue, Niemann et al. (2007) provide the first structural evidence that InlB does not compete for the same interaction site on Met as the natural ligand HGF.
Veiga
Esteban
E
Institut Pasteur, Unité des Interactions Bactéries-Cellules, Paris, F-75015 France. eveiga@pasteur.fr
Cossart
Pascale
P
D001426:Bacterial Proteins / Q000737:chemistry*; D017228:Hepatocyte Growth Factor / Q000378:metabolism; D006801:Humans; D000090263:Leucine-Rich Repeat Proteins; D008089:Listeria monocytogenes / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D008954:Models, Biological; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000378:metabolism; D019859:Proto-Oncogene Proteins c-met / Q000737:chemistry*
D001426:Bacterial Proteins; D000090263:Leucine-Rich Repeat Proteins; D008565:Membrane Proteins; D011506:Proteins; C095768:inlB protein, Listeria monocytogenes; D017228:Hepatocyte Growth Factor; D019859:Proto-Oncogene Proteins c-met