1WFC

STRUCTURE OF APO, UNPHOSPHORYLATED, P38 MITOGEN ACTIVATED PROTEIN KINASE P38 (P38 MAP KINASE) THE MAMMALIAN HOMOLOGUE OF THE YEAST HOG1 PROTEIN

1WFC の概要

• エントリーDOI: 10.2210/pdb1wfc/pdb
• 分子名称: MITOGEN-ACTIVATED PROTEIN KINASE P38 (2 entities in total)
• 機能のキーワード: p38 map kinase, serine/threonine protein kinase, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm (By similarity): Q16539
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41998.94

構造登録者

Wilson, K.P.,Fitzgibbon, M.J.,Caron, P.R.,Griffith, J.P.,Chen, W.,Mccaffrey, P.G.,Chambers, S.P.,Su, M.S.-S. (登録日: 1996-09-13, 公開日: 1997-09-19, 最終更新日: 2024-02-14)

主引用文献

Wilson, K.P.,Fitzgibbon, M.J.,Caron, P.R.,Griffith, J.P.,Chen, W.,McCaffrey, P.G.,Chambers, S.P.,Su, M.S.
Crystal structure of p38 mitogen-activated protein kinase.
J.Biol.Chem., 271:27696-27700, 1996

PubMed Abstract: p38 mitogen-activated protein kinase is activated by environmental stress and cytokines and plays a role in transcriptional regulation and inflammatory responses. The crystal structure of the apo, unphosphorylated form of p38 kinase has been solved at 2.3 A resolution. The fold and topology of p38 is similar to ERK2 (Zhang, F., Strand, A., Robbins, D., Cobb, M. H., and Goldsmith, E. J. (1994) Nature 367, 704-711). The relative orientation of the two domains of p38 kinase is different from that observed in the active form of cAMP-dependent protein kinase. The twist results in a misalignment of the active site of p38, suggesting that the orientation of the domains would have to change before catalysis could proceed. The residues that are phosphorylated upon activation of p38 are located on a surface loop that occupies the peptide binding channel. Occlusion of the active site by the loop, and misalignment of catalytic residues, may account for the low enzymatic activity of unphosphorylated p38 kinase.

PubMed: 8910361
DOI: 10.1074/jbc.271.44.27696

実験手法

X-RAY DIFFRACTION (2.3 Å)