Insulin-like growth factor receptors (IGFR) are transmembrane receptors which are stimulated by insulin-like growth factors (IGF). IGFR contains 2 extracellular α chains and 2 transmembranal β chains. Upon binding of IGF, a tyrosine in the β chain becomes autophosphorylated and triggers a cascade of intracellular signaling.
3D structures of insulin-like growth factor receptor
IGFR I
1igr – hIGFR I domains 1-3 – human
2cnj - hIGFR I domain 11 - NMR
1q25 - bIGFR I domains 1-3 – bovine
1jqh, 1p4o - hIGFR I kinase domain (mutant)
1m7n - hIGFR I kinase domain
1k3a - hIGFR I kinase domain + insulin receptor substrate peptide
2oj9, 2zm3, 3d94, 3f5p, 3i81, 3lvp, 3nw5, 3nw6, 3nw7, 3lw0, 3qqu, 3o23 - hIGFR I kinase domain + inhibitor
1syo, 1sz0 - bIGFR I domains 1-3 + mannose-6-phosphate
IGFR II
1gqb - hIGFR II
2kva - hIGFR II domain 5 – NMR
2l2a - hIGFR II domains 11 (mutant) - NMR
2kvb - hIGFR II domain 5 + inhibitor – NMR
2v5n - hIGFR II domains 11-12
2v5o - hIGFR II domains 11-14
2v5p - hIGFR II domains 11-13 + IGF II
2l29 - hIGFR II domain 11 + IGF II - NMR
1gp0, 1gp3, 1e6f - hIGFR II IGF II-binding domain
