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Numerous receptors have intrinsic or tightly related enzyme activity. On the required of ligand to their extracellular face like receptors undergo a conformational change and activate an enzyme activity. In case of the insulin receptor that is a complex of two α- and two β-subunits held together through disulfide bonds the polypeptide hormone insulin the ligand binds to the extracellular face of the α-subunits. The receptor then undergoes a conformational modify leading to the autophosphorylation of the cytosolic domain of the β-subunit. By the specifically hydroxyl groups in the side chains of certain tyrosine residues are phosphorylated with ATP being the phosphate donor. Phosphorylated receptor is then identify by other proteins in the cytosol which in turn modulate various intracellular events permitting the cell to respond to the hormone appropriately. Additionally, β-subunit can straight phosphorylate other goal proteins within the cell.
figure: Signal transduction through an enzyme-linked receptor such as the insulin receptor.
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