2erk
From Proteopedia
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PHOSPHORYLATED MAP KINASE ERK2
Overview
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.
About this Structure
2ERK is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Activation mechanism of the MAP kinase ERK2 by dual phosphorylation., Canagarajah BJ, Khokhlatchev A, Cobb MH, Goldsmith EJ, Cell. 1997 Sep 5;90(5):859-69. PMID:9298898
Page seeded by OCA on Thu Feb 21 17:13:51 2008
