Molecular Dynamics Study on the Activation Mechanism of p47phox in the Auto-Inhibited Form

DOI Web Site Web Site 49 References
  • WATANABE Yoko
    Department of Applied Chemistry, Graduate School of Engineering, Tohoku University
  • TSUBOI Hideyuki
    Department of Applied Chemistry, Graduate School of Engineering, Tohoku University
  • KOYAMA Michihisa
    Department of Applied Chemistry, Graduate School of Engineering, Tohoku University PRESTO, Japan Science and Technology Agency
  • KUBO Momoji
    Department of Applied Chemistry, Graduate School of Engineering, Tohoku University New Industry Creation Hatchery Center, Tohoku University
  • A. DEL CARPIO Carlos
    Department of Applied Chemistry, Graduate School of Engineering, Tohoku University
  • ICHIISHI Eiichiro
    New Industry Creation Hatchery Center, Tohoku University
  • KOHNO Masahiro
    New Industry Creation Hatchery Center, Tohoku University
  • MIYAMOTO Akira
    Department of Applied Chemistry, Graduate School of Engineering, Tohoku University New Industry Creation Hatchery Center, Tohoku University

Bibliographic Information

Other Title
  • 自己阻害型ｐ４７｀ｐｈｏｘ´の活性化機構に関する分子シミュレーション
  • 自己阻害型p47phoxの活性化機構に関する分子シミュレーション
  • ジコ ソガイガタ p47phox ノ カッセイカ キコウ ニ カンスル ブンシ シミュレーション

Search this article

Abstract

The phagocyte NADPH oxidase complex plays a crucial role in host defense against microbial infection through the production of reactive oxygen species. Key to the activation of NADPH oxidase is cytoplasmic subunit p47phox, which includes tandem SH3 domains and the polybasic region (Figure 1). Recently, the crystal structures of the active and inactive states of p47phox were determined, conformational change that mediates these two structures remains to be elucidated. Our simulations revealed that phosphorylations of Ser303, 304, and 328, which are important for activation of p47phox, contribute to structural changes in the region that is isolated from these serine residues. Additionally, it is concluded that the ligand exchange of p47phox in activation of NADPH oxidase is induced by interaction between the membrane subunit p22phox and N-terminal SH3 domain of p47phox that was exposed to solvent by phosphorylations.

Journal

References(49)*help

See more

Keywords

Details 詳細情報について

Report a problem

Back to top