Insulin-like growth factor receptor (IGF1R) is a cell surface, tyrosine kinase receptor that can be activated by IGF1, IGF2, and insulin¹.

IGF receptors are tyrosine kinase-containing heterotetramers that are linked to numerous cytoplasmic signaling cascades and have important roles in various cellular functions. IGF1R displays potent anti-apoptotic, pro-survival capacities and plays a key role in malignant transformation by regulating MAPK and PI3K/AKT signaling pathways. IGF1R regulators are identified as a candidate therapeutic targets in cancer and growth-related diseases^1,2.

IGF1R and insulin receptor (IR) are closely related, and share 57% sequence identity and high structural similarity. Each IGF1R and IR receptor consists of the L1, CR, L2, FnIII-1,-2,-3, transmembrane (TM), and kinase domain. Two such protomers are linked by multiple disulfide bonds, forming a stable, covalent dimer. Upon ligand binding, the dimer undergoes significant conformational changes which facilitate its further signal transduction cascade³.