2UZX

Structure of the human receptor tyrosine kinase Met in complex with the Listeria monocytogenes invasion protein InlB: Crystal form I

Summary for 2UZX

• Entry DOI: 10.2210/pdb2uzx/pdb
• Related: 1D0B 1FYR 1H6T 1M9S 1OTM 1OTN 1OTO 1R0P 1R1W 1SHY 1SSL 1UX3 2CEW 2G15 2UZY
• Descriptor: INTERNALIN B, HEPATOCYTE GROWTH FACTOR RECEPTOR (2 entities in total)
• Functional Keywords: signaling protein/receptor, leucine rich repeat, receptor ectodomain, hepatocyte growth factor receptor, signaling protein, atp-binding, transferase, polymorphism, glycoprotein, virulence factor, disease mutation, nucleotide-binding, transmembrane, proto-oncogene, phosphorylation, leucine-rich repeat, alternative splicing, tyrosine-protein kinase, chromosomal rearrangement, lrr, hgfr, kinase, membrane, receptor, internalin, signaling protein-receptor complex
• Biological source: LISTERIA MONOCYTOGENES; More
• Total number of polymer chains: 4
• Total formula weight: 228293.73

Authors

Niemann, H.H.,Jager, V.,Butler, P.J.G.,Van Den Heuvel, J.,Schmidt, S.,Ferraris, D.,Gherardi, E.,Heinz, D.W. (deposition date: 2007-05-02, release date: 2007-08-07, Last modification date: 2023-12-13)

Primary citation

Niemann, H.H.,Jager, V.,Butler, P.J.G.,Van Den Heuvel, J.,Schmidt, S.,Ferraris, D.,Gherardi, E.,Heinz, D.W.
Structure of the Human Receptor Tyrosine Kinase met in Complex with the Listeria Invasion Protein Inlb
Cell(Cambridge,Mass.), 130:235-, 2007

PubMed Abstract: 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.

PubMed: 17662939
DOI: 10.1016/J.CELL.2007.05.037

Experimental method

X-RAY DIFFRACTION (2.8 Å)