2OKR

Crystal Structure of the P38a-MAPKAP kinase 2 Heterodimer

2OKR の概要

• エントリーDOI: 10.2210/pdb2okr/pdb
• 関連するPDBエントリー: 2ONL
• 分子名称: Mitogen-activated protein kinase 14, MAP kinase-activated protein kinase 2 (3 entities in total)
• 機能のキーワード: kinase, nls, nes, heterodimer, docking groove, transferase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm (By similarity): Q16539
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 89622.90

構造登録者

Ter Haar, E. (登録日: 2007-01-17, 公開日: 2007-02-06, 最終更新日: 2023-08-30)

主引用文献

ter Haar, E.,Prabakhar, P.,Liu, X.,Lepre, C.
Crystal structure of the P38alpha-MAPKAP kinase 2 heterodimer.
J.Biol.Chem., 282:9733-9739, 2007

PubMed Abstract: The p38 signaling pathway is activated in response to cell stress and induces production of proinflammatory cytokines. P38alpha is phosphorylated and activated in response to cell stress by MKK3 and MKK6 and in turn phosphorylates a number of substrates, including MAPKAP kinase 2 (MK2). We have determined the crystal structure of the unphosphorylated p38alpha-MK2 heterodimer. The C-terminal regulatory domain of MK2 binds in the docking groove of p38alpha, and the ATP-binding sites of both kinases are at the heterodimer interface. The conformation suggests an extra mechanism in addition to the regulation of the p38alpha and MK2 phosphorylation states that prevents phosphorylation of substrates in the absence of cell stress. Addition of constitutively active MKK6-DD results in rapid phosphorylation of the p38alpha-MK2 heterodimer.

PubMed: 17255097
DOI: 10.1074/jbc.M611165200

実験手法

X-RAY DIFFRACTION (2 Å)