Article
Activation of the Lck tyrosine protein kinase by the Herpesvirus saimiri tip protein involves two binding interactions.
Virology - 25 Oct 2000
Hartley D A, Amdjadi K, Hurley T R, Lund T C, Medveczky P G, Sefton B M
Abstract excerpt
The Tip protein of Herpesvirus saimiri strain 484C binds to and activates the Lck tyrosine protein kinase. Two sequences in the Tip protein were previously shown to be involved in binding to Lck. A proline-rich region, residues 132-141, binds to the SH3 domain of the Lck protein. We show here that the other Lck-binding domain, residues 104-113, binds to the carboxyl-terminal half of Lck and that this binding does...
Topics
- Binding Sites
- Cell Line
- DNA-Binding Proteins
- Enzyme Activation
- Herpesvirus 2, Saimiriine
- Humans
- Jurkat Cells
- Lymphocyte Specific Protein Tyrosine Kinase p56(lck)
- Models, Molecular
- Mutation
- Phosphoproteins