Insulin receptor (IR) is a transmembrane receptor activated by insulin, IGF-I and IGF-II. IR is important for the regulation of glucose homeostasis and its malfunction can cause diabetics and cancer. The IR is a dimer where each monomer contains 8 distinct domains. The beta-chain contains a tyrosine kinase catalytic domain (TK).
3D structures of insulin receptor
1irk – hIR TK domain – human
1i44, 1p14 – hIR TK domain (mutant)
2hr7 – hIR domains 1-3
2mfr – hIR transmembrane domain - NMR
4xlv - hIR TK domain (mutant) + ATP derivative
1ir3 - hIR TK domain (mutant) + ATP analog + peptide
3bu5, 3bu6 - hIR TK domain + ATP + peptide
3bu3 - hIR TK domain + peptide
1gag, 2z8c - hIR TK domain (mutant) + peptide
3ekk, 3ekn, 4ibm - hIR TK domain (mutant) + inhibitor
3eta - hIR TK domain + inhibitor
2dtg, 3loh - hIR ectodomain (mutant) + antibody
2auh – hIR TK domain + growth factor receptor-bound protein 14
2b4s - hIR TK domain + tyrosine-protein phosphatase
1rqq – hIR TK domain (mutant) + adaptor protein PS
