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Activation mechanism of the MAP kinase ERK2 by dual phosphorylation.
The structure of the active form of the MAP kinase ERK2 has been solved, phosphorylated on a threonine and a tyrosine residue within the phosphorylation lip. The lip is refolded, bringing the phosphothreonine and phosphotyrosine into alignment with surface arginine-rich binding sites. Conformational changes occur in the lip and neighboring structures, including the P+1 site, the MAP kinase insertion, the C-terminal extension, and helix C. Domain rotation and remodeling of the proline-directed P+1 specificity pocket account for the activation. The conformation of the P+1 pocket is similar to a second proline-directed kinase, CDK2-CyclinA, thus permitting the origin of this specificity to be defined. Conformational changes outside the lip provide loci at which the state of phosphorylation can be felt by other cellular components.[1]References
- Activation mechanism of the MAP kinase ERK2 by dual phosphorylation. Canagarajah, B.J., Khokhlatchev, A., Cobb, M.H., Goldsmith, E.J. Cell (1997) [Pubmed]
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