3PY3

Crystal structure of phosphorylated p38alpha MAP kinase

3PY3 の概要

• エントリーDOI: 10.2210/pdb3py3/pdb
• 分子名称: Mitogen-activated protein kinase 14 (2 entities in total)
• 機能のキーワード: kinase, transferase, phosphorylation
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Cytoplasm: P47811
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43669.47

構造登録者

Zhang, Y.Y.,Wu, J.W.,Wang, Z.X. (登録日: 2010-12-11, 公開日: 2011-03-16, 最終更新日: 2024-11-20)

主引用文献

Zhang, Y.Y.,Wu, J.W.,Wang, Z.X.
Mitogen-activated Protein Kinase (MAPK) Phosphatase 3-mediated Cross-talk between MAPKs ERK2 and p38{alpha}.
J.Biol.Chem., 286:16150-16162, 2011

PubMed Abstract: MAPK phosphatase 3 (MKP3) is highly specific for ERK1/2 inactivation via dephosphorylation of both phosphotyrosine and phosphothreonine critical for enzymatic activation. Here, we show that MKP3 is able to effectively dephosphorylate the phosphotyrosine, but not phosphothreonine, in the activation loop of p38α in vitro and in intact cells. The catalytic constant of the MKP3 reaction for p38α is comparable with that for ERK2. Remarkably, MKP3, ERK2, and phosphorylated p38α can form a stable ternary complex in solution, and the phosphatase activity of MKP3 toward p38α substrate is allosterically regulated by ERK2-MKP3 interaction. This suggests that MKP3 not only controls the activities of ERK2 and p38α but also mediates cross-talk between these two MAPK pathways. The crystal structure of bisphosphorylated p38α has been determined at 2.1 Å resolution. Comparisons between the phosphorylated MAPK structures reveal the molecular basis of MKP3 substrate specificity.

PubMed: 21454500
DOI: 10.1074/jbc.M110.203786

実験手法

X-RAY DIFFRACTION (2.1 Å)