Article
Active mutants of the TCR-mediated p38α alternative activation site show changes in the phosphorylation lip and DEF site formation.
Journal of molecular biology - 4 Feb 2011
Tzarum Netanel, Diskin Ron, Engelberg David, Livnah Oded
Abstract excerpt
The p38α mitogen-activated protein kinase is commonly activated by dual (Thr and Tyr) phosphorylation catalyzed by mitogen-activated protein kinase kinases. However, in T-cells, upon stimulation of the T-cell receptor, p38α is activated via an alternative pathway, involving its phosphorylation by zeta-chain-associated protein kinase 70 on Tyr323, distal from the phosphorylation lip. Tyr323-phosphorylated p38α is...
Topics
- Amino Acid Sequence
- Catalytic Domain
- Crystallography, X-Ray
- Enzyme Activation
- Humans
- Mitogen-Activated Protein Kinase 14
- Molecular Sequence Data
- Mutation
- Phosphorylation
- Protein Conformation