2ERK
PHOSPHORYLATED MAP KINASE ERK2
2ERK の概要
| エントリーDOI | 10.2210/pdb2erk/pdb |
| 分子名称 | EXTRACELLULAR SIGNAL-REGULATED KINASE 2 (2 entities in total) |
| 機能のキーワード | phosphotransferase, kinase, serine/threonine-protein kinase |
| 由来する生物種 | Rattus norvegicus (Norway rat) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 42390.46 |
| 構造登録者 | |
| 主引用文献 | 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 Cited by 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: 9298898DOI: 10.1016/S0092-8674(00)80351-7 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.4 Å) |
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