Article
The regulatory role of known tyrosine autophosphorylation sites of the insulin receptor kinase domain. An assessment by replacement with neutral and negatively charged amino acids.
The Journal of biological chemistry - 15 Jan 1991
Zhang B, Tavaré J M, Ellis L, Roth R A
Abstract excerpt
Autophosphorylation of the insulin receptor has been previously documented to activate the phosphotransferase activity of the receptor from 20- to 200-fold. Biochemical studies have correlated activation of the receptor kinase with the autophosphorylation of tyrosines residues 1158, 1162, and 1163. To further assess the role of these 3 tyrosines in the activation process, we have studied the effect of their...
Topics
- Amino Acids
- Blotting, Western
- Cells, Cultured
- DNA
- Electrophoresis, Polyacrylamide Gel
- Humans
- Insulin
- Mutation
- Peptide Mapping
- Phosphorylation
- Protein-Tyrosine Kinases