2ERK

PHOSPHORYLATED MAP KINASE ERK2

Summary for 2ERK

• Entry DOI: 10.2210/pdb2erk/pdb
• Descriptor: EXTRACELLULAR SIGNAL-REGULATED KINASE 2 (2 entities in total)
• Functional Keywords: phosphotransferase, kinase, serine/threonine-protein kinase
• Biological source: Rattus norvegicus (Norway rat)
• Total number of polymer chains: 1
• Total formula weight: 42390.46

Authors

Canagarajah, B.J.,Goldsmith, E.J. (deposition date: 1997-06-26, release date: 1998-07-01, Last modification date: 2024-11-06)

Primary citation

Canagarajah, B.J.,Khokhlatchev, A.,Cobb, M.H.,Goldsmith, E.J.
Activation mechanism of the MAP kinase ERK2 by dual phosphorylation.
Cell(Cambridge,Mass.), 90:859-869, 1997

PubMed 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.

PubMed: 9298898
DOI: 10.1016/S0092-8674(00)80351-7

Experimental method

X-RAY DIFFRACTION (2.4 Å)