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Insulin receptor inhibitors act on the tyrosine kinase receptor that relays insulin signals into cells. Two groups reported the human insulin receptor sequence in 1985 and placed it in the tyrosine kinase family of oncogenes. The receptor is a disulfide-linked dimer of alpha and beta subunits, and insulin binding triggers autophosphorylation of the beta subunits. Insulin receptor substrate proteins then couple the kinase to glucose uptake, glycogen synthesis and cell growth. Most compounds here are dual inhibitors that block the insulin receptor together with the insulin-like growth factor 1 receptor (IGF-1R). Examples are BMS-536924, GSK1904529A and AG-1024, while NVP-TAE 226 also inhibits focal adhesion kinase (FAK).
Insulin receptor (1142-1153), pTyr1150 is a biological active peptide. (Peptide used as insulin receptor tyrosine kinase substrate.)
