2DYB

The crystal structure of human p40(phox)

2DYB の概要

• エントリーDOI: 10.2210/pdb2dyb/pdb
• 分子名称: Neutrophil cytosol factor 4 (1 entity in total)
• 機能のキーワード: p40(phox), nadph oxidase, oxidoreductase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q15080
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 78661.52

構造登録者

Honbou, K. (登録日: 2006-09-08, 公開日: 2007-01-23, 最終更新日: 2024-10-16)

主引用文献

Honbou, K.,Minakami, R.,Yuzawa, S.,Takeya, R.,Suzuki, N.N.,Kamakura, S.,Sumimoto, H.,Inagaki, F.
Full-length p40phox structure suggests a basis for regulation mechanism of its membrane binding.
Embo J., 26:1176-1186, 2007

PubMed Abstract: The superoxide-producing phagocyte NADPH oxidase is activated during phagocytosis to destroy ingested microbes. The adaptor protein p40phox associates via the PB1 domain with the essential oxidase activator p67phox, and is considered to function by recruiting p67phox to phagosomes; in this process, the PX domain of p40phox binds to phosphatidylinositol 3-phosphate [PtdIns(3)P], a lipid abundant in the phagosomal membrane. Here we show that the PtdIns(3)P-binding activity of p40phox is normally inhibited by the PB1 domain both in vivo and in vitro. The crystal structure of the full-length p40phox reveals that the inhibition is mediated via intramolecular interaction between the PB1 and PX domains. The interface of the p40phox PB1 domain for the PX domain localizes on the opposite side of that for the p67phox PB1 domain, and thus the PB1-mediated PX regulation occurs without preventing the PB1-PB1 association with p67phox.

PubMed: 17290225
DOI: 10.1038/sj.emboj.7601561

実験手法

X-RAY DIFFRACTION (3.15 Å)