2erk | pdb_00002erk

PHOSPHORYLATED MAP KINASE ERK2

spinqualitylabelsall models 2erk, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2erk is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: PTR, TPO Gene: ERK2 (Rattus norvegicus) Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Michael Roberts/BIOL115/ERK2 Mitogen-activated protein kinase

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