Function
Insulin receptor (IR) is a transmembrane receptor activated by insulin, insulin-like growth factor I and II[1]. The IR is a dimer where each monomer contains 8 distinct domains. Residues 28-337 are the L1-CR domain. The β-chain contains a tyrosine kinase catalytic domain (TK) residues 1005-1310. For more details see Student Projects for UMass Chemistry 423 Spring 2012-1.
Disease
IR is important for the regulation of glucose homeostasis and its malfunction can cause diabetes and cancer. IR is overexpressed in cancer[2].
Structural highlights
(PDB entry 3bu5).
TK domain of IR contains an activation loop and a catalytic loop and . The bound IR substrate 2 peptide tyrosine is the phosphorylated residue[3].
In type 2 diabetes, the TK domain is thought to be down-regulated through phosphorylation of by protein kinease C[4].
. Water molecules shown as red spheres.
See also Insulin Receptor - kinase domain (Hebrew) and Insulin receptor (Hebrew).
3D structures of insulin receptor
Insulin receptor 3D structures
