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. 1997 Sep 5;90(5):859-69.
doi: 10.1016/s0092-8674(00)80351-7.

Activation mechanism of the MAP kinase ERK2 by dual phosphorylation

B J Canagarajah  1 , A Khokhlatchev, M H Cobb, E J Goldsmith
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Free article

Activation mechanism of the MAP kinase ERK2 by dual phosphorylation

B J Canagarajah et al. Cell. .
Free article

Abstract

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.

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