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• W2100891825 startingPage "12039" @default.
• W2100891825 abstract "Little is known about the large ectodomain of MET, the product of the c- met protooncogene and receptor for hepatocyte growth factor/scatter factor (HGF/SF). Here, we establish by deletion mutagenesis that the HGF/SF and heparin-binding sites of MET are contained within a large N-terminal domain spanning the α-chain (amino acids 25–307) and the first 212 amino acids of the β-chain (amino acids 308–519). Neither the cystine-rich domain (amino acids 520–561) nor the C-terminal half of MET (amino acids 562–932) bind HGF/SF or heparin directly. The MET ectodomain, which behaves as a rod-shaped monomer with a large Stokes radius in solution, binds HGF/SF in the absence or presence of heparin, and forms a stable HGF/SF–heparin–MET complex with 1:1:1 stoichiometry. We also show that the ligand-binding domain adopts a β-propeller fold, which is similar to the N-terminal domain of αV integrin, and that the C-terminal half contains four Ig domains (amino acids 563–654, 657–738, 742–836, and 839–924) of the unusual structural E set, which could be modeled on bacterial enzymes. Our studies provide 3D models and a functional map of the MET ectodomain. They have broad implications for structure-function of the MET receptor and the related semaphorin and plexin proteins." @default.
• W2100891825 created "2016-06-24" @default.
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• W2100891825 date "2003-10-03" @default.
• W2100891825 modified "2023-10-10" @default.
• W2100891825 title "Functional map and domain structure of MET, the product of the c- <i>met</i> protooncogene and receptor for hepatocyte growth factor/scatter factor" @default.
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• W2100891825 doi "https://doi.org/10.1073/pnas.2034936100" @default.
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