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2ERK

PHOSPHORYLATED MAP KINASE ERK2

2ERK の概要
エントリーDOI10.2210/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
Canagarajah, B.J.,Goldsmith, E.J. (登録日: 1997-06-26, 公開日: 1998-07-01, 最終更新日: 2024-11-06)
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: 9298898
DOI: 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)
構造検証レポート
Validation report summary of 2erk
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-08に公開中

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