Human insulin receptors mutated at the ATP-binding site lack protein tyrosine kinase activity and fail to mediate postreceptor effects of insulin.

@article{Chou1987HumanIR,
  title={Human insulin receptors mutated at the ATP-binding site lack protein tyrosine kinase activity and fail to mediate postreceptor effects of insulin.},
  author={Chen Kung Chou and Thomas J. Dull and David Stark Russell and R Gherzi and David Edward Lebwohl and Axel Ullrich and O. M. Rosen},
  journal={The Journal of biological chemistry},
  year={1987},
  volume={262 4},
  pages={1842-7}
}
Transfected Chinese hamster ovary cell lines were developed that expressed equivalent numbers of either normal human receptor or receptor that had alanine substituted for Lys-1018 in the ATP-binding domain of the beta subunit. The mutated receptor was processed into subunits and bound insulin but lacked protein tyrosine kinase activity. Five effects of insulin were assayed: deoxyglucose uptake, S6 kinase activity, endogenous protein-tyrosine phosphorylation, glycogen synthesis, and thymidine… CONTINUE READING