Hepatocyte growth factor receptor

Some of the most important aspects of this RTK are the tyrosines at position 1234 and 1235. These two residues will become phosphorylated upon activation of the protein. There is another pair of important . Studies with mice have shown that these tyrosines are necessary for normal c-met signaling. When these two tyrosines were substituted with with phenylalenine, the mice had an embryonically lethal phenotype and defects were found in placenta, liver, muscles and nerves. ^[3] In a wild type c-met, these sites will become phosphorylated and act as docking sites for many different transducers and adapters. ^[4] The c-met kinase domain is very similar to a typical protein kinase structure.

The N-terminal of the protein contains many and is linked through a hinge to the C lobe, which is full of α helices. This particular kinase domain is very similar to the domains of the insulin receptor kinase and fibroblast growth factor receptor kinase. One main difference is that the c-met structure has an helix between residues 1060-1069 not present in FGFRK or IRK. ^[5]

spinqualitylabelsall models Structure of Hepatocyte Growth Factor Receptor Tyrosine Kinase Domain in complex with K-252a (PDB entry 1r0p) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image