2uzx
STRUCTURE OF THE HUMAN RECEPTOR TYROSINE KINASE MET IN COMPLEX WITH THE LISTERIA MONOCYTOGENES INVASION PROTEIN INLB: CRYSTAL FORM I
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OverviewOverview
The tyrosine kinase Met, the product of the c-met proto-oncogene and the, receptor for hepatocyte growth factor/scatter factor (HGF/SF), mediates, signals critical for cell survival and migration. The human pathogen, Listeria monocytogenes exploits Met signaling for invasion of host cells, via its surface protein InlB. We present the crystal structure of the, complex between a large fragment of the human Met ectodomain and the, Met-binding domain of InlB. The concave face of the InlB leucine-rich, repeat region interacts tightly with the first immunoglobulin-like domain, of the Met stalk, a domain which does not bind HGF/SF. A second contact, between InlB and the Met Sema domain locks the otherwise flexible receptor, in a rigid, signaling competent conformation. Full Met activation requires, the additional C-terminal domains of InlB which induce heparin-mediated, receptor clustering and potent signaling. Thus, although it elicits a, similar cellular response, InlB is not a structural mimic of HGF/SF.
About this StructureAbout this Structure
2UZX is a Protein complex structure of sequences from Homo sapiens and Listeria monocytogenes. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the Human Receptor Tyrosine Kinase Met in Complex with the Listeria Invasion Protein InlB., Niemann HH, Jager V, Butler PJ, van den Heuvel J, Schmidt S, Ferraris D, Gherardi E, Heinz DW, Cell. 2007 Jul 27;130(2):235-246. PMID:17662939
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