Article
A new class of mutations reveals a novel function for the original phosphatidylinositol 3-kinase binding site.
Proceedings of the National Academy of Sciences of the United States of America - 5 Aug 2003
Hong Y Kate, Mikami Aki, Schaffhausen Brian, Jun Toni, Roberts Thomas M
Abstract excerpt
Previous studies have demonstrated that the specificity of Src homology 2 (SH2) and phosphotyrosine-binding domain interactions are mediated by phosphorylated tyrosines and their neighboring amino acids. Two of the first phosphotyrosine-based binding sites were found on middle T antigen of polyoma virus. Tyr-250 acts as a binding site for ShcA, whereas Tyr-315 forms a binding site for the SH2 domain of the p85...
Topics
- Alanine
- Alleles
- Amino Acid Sequence
- Animals
- Binding Sites
- Immunoblotting
- Mice
- Mice, Inbred BALB C
- Molecular Sequence Data
- Mutation
- Phenylalanine
- Phosphatidylinositol 3-Kinases
- Plasmids
- Precipitin Tests