Structure-function relationship of the insulin-like growth factor-I receptor tyrosine kinase.
作者： M Grønborg , B.S. Wulff , J.S. Rasmussen , T Kjeldsen , S Gammeltoft
DOI: 10.1016/S0021-9258(19)49481-7
关键词:
摘要: Insulin-like growth factor I (IGF-I) and insulin receptors are structurally similar with ligand-stimulated tyrosine kinase activity in their cytoplasmic domains. The function of the receptor signal transduction has been studied extensively contrast to IGF-I kinase. In present study we have analyzed regulatory carboxyl-terminal domains mitogenic signaling by overexpression mutant mouse NIH-3T3 fibroblasts. A receptor, which 3 tyrosines (Tyr1131, Tyr1135, Tyr1136) analogous three major autophosphorylation sites were replaced phenylalanines, was devoid vivo vitro inactive respect internalization stimulation thymidine incorporation. Another lacks 49 amino acids (residues 1289-1337) beta-subunit, fully active. Our data suggest that structure-function relationship activation is receptor.
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