1NVU

Structural evidence for feedback activation by RasGTP of the Ras-specific nucleotide exchange factor SOS

1NVU の概要

• エントリーDOI: 10.2210/pdb1nvu/pdb
• 関連するPDBエントリー: 1BDK 1NVV 1NVW 1NVX
• 分子名称: Transforming protein p21/H-RAS-1, Son of sevenless protein homolog 1, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: proto-oncogene, gtp binding, guanine nucleotide release factor, signaling protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cell membrane; Lipid-anchor; Cytoplasmic side: P01112
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 95277.40

構造登録者

Margarit, S.M.,Sondermann, H.,Hall, B.E.,Nagar, B.,Hoelz, A.,Pirruccello, M.,Bar-Sagi, D.,Kuriyan, J. (登録日: 2003-02-04, 公開日: 2003-04-01, 最終更新日: 2023-08-16)

主引用文献

Margarit, S.M.,Sondermann, H.,Hall, B.E.,Nagar, B.,Hoelz, A.,Pirruccello, M.,Bar-Sagi, D.,Kuriyan, J.
Structural evidence for feedback activation by RasGTP of the Ras-specific nucleotide exchange factor SOS
Cell(Cambridge,Mass.), 112:685-695, 2003

PubMed Abstract: Growth factor receptors activate Ras by recruiting the nucleotide exchange factor son of sevenless (SOS) to the cell membrane, thereby triggering the production of GTP-loaded Ras. Crystallographic analyses of Ras bound to the catalytic module of SOS have led to the unexpected discovery of a highly conserved Ras binding site on SOS that is located distal to the active site and is specific for Ras.GTP. The crystal structures suggest that Ras.GTP stabilizes the active site of SOS allosterically, and we show that Ras.GTP forms ternary complexes with SOS(cat) in solution and increases significantly the rate of SOS(cat)-stimulated nucleotide release from Ras. These results demonstrate the existence of a positive feedback mechanism for the spatial and temporal regulation of Ras.

PubMed: 12628188
DOI: 10.1016/S0092-8674(03)00149-1

実験手法

X-RAY DIFFRACTION (2.2 Å)