24 nucleotide stem-loop, u2 snrnp hairpin iv. U2 a'; Chain A
Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A domain 2
Transferase(Phosphotransferase); domain 1
ATP:protein-tyrosine O-phosphotransferase (ambiguous)
insulin receptor protein-tyrosine kinase
;TYR 1165;TYR 1166(auto-phosphorylation)
PTR 1131;PTR 1135;PTR 1136(auto-phosphorylation)
TYR 1158;TYR 1162;TYR 1163(auto-phosphorylation)
TYR 1131;TYR 1135;TYR 1136(auto-phosphorylation)
Analysis of the interaction of IGF-I analogs with the IGF-I receptor and IGF binding proteins.
The insulin-like growth factor-I receptor. Structure, ligand-binding mechanism and signal transduction.
Tyrosine residues in the C-terminal domain of the insulin-like growth factor-I receptor mediate mitogenic and tumorigenic signals.
Crystallization of the first three domains of the human insulin-like growth factor-1 receptor.
Crystal structure of the first three domains of the type-1 insulin-like growth factor receptor.
C-terminal Src kinase associates with ligand-stimulated insulin-like growth factor-I receptor.
Autophosphorylation of the insulin-like growth factor I receptor cytoplasmic domain.
Regulation of survival signals from the insulin-like growth factor-I receptor.
Cys 786 and Cys 776 in the posttranslational processing of the insulin and IGF-I receptors.
Specificity in ligand binding and intracellular signalling by insulin and insulin-like growth factor receptors.
Dimerization-induced activation of soluble insulin/IGF-1 receptor kinases: an alternative mechanism of activation.
A PDZ domain protein interacts with the C-terminal tail of the insulin-like growth factor-1 receptor but not with the insulin receptor.
Cooperative regulation of the invasive and metastatic phenotypes by different domains of the type I insulin-like growth factor receptor beta subunit.
Alanine scanning mutagenesis of a type 1 insulin-like growth factor receptor ligand binding site.
The three dimensional structure of the type I insulin-like growth factor receptor.
Structure and autoregulation of the insulin-like growth factor 1 receptor kinase.
Structure-function studies of an IGF-I analogue that can be chemically cleaved to a two-chain mini-IGF-I.
Crystal structure of bisphosphorylated IGF-1 receptor kinase: insight into domain movements upon kinase activation.
Crystal structure of the Apo, unactivated insulin-like growth factor-1 receptor kinase. Implication for inhibitor specificity.
The E.C. was transferred from 2.7.1.112 to 2.7.10.1. This protein is a receptor enzyme, insulin-like growth factor I receptor, composed of two chains, alpha and beta. PDB structure, 1igr, corresponds to the N-terminal domains of the alpha chain. The beta chain is composed of an extracellular reagion, transmembrane region, and a cytoplasmic region. The extracellular region contains a fibronectin type-III domain, whilst the cytoplasmic region has got a kinase domain. PDB structures, 1jqh, 1k3a, 1m7n & 1p4o, correspond to the kinase domain. According to the literature [17] & [19], Asp1105 (of PDB entry 1k3a) seemes to be a general base, which can activate the acceptor group, the hydroxyl group of substrate tyrosine, which in turn would make a nucleophilic attack on the transferred group, gamma-phosphate group of ATP. Arg1109 also seems to interact with both the general base and the acceptor hydroxyl group. Although two magnesium ions are coordinated to the beta- and gamma-phosphates of ATP analogue in a homologous receptor enzyme, Insulin receptor kinase (see M00129), only one magnesium ion is coordinated by the alpha- and gamma-phosphates and two water molecules (see [19]).