1XD2
Crystal Structure of a ternary Ras:SOS:Ras*GDP complex
1XD2 の概要
| エントリーDOI | 10.2210/pdb1xd2/pdb |
| 関連するPDBエントリー | 1BKD 1NVU 1NVV 1NVW 1NVX 1XD4 |
| 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 | ras:sos complex, ras-nucleotide exchange factor complex, 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 P01112 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 95293.68 |
| 構造登録者 | Sondermann, H.,Soisson, S.M.,Boykevisch, S.,Yang, S.S.,Bar-Sagi, D.,Kuriyan, J. (登録日: 2004-09-03, 公開日: 2004-11-02, 最終更新日: 2023-08-23) |
| 主引用文献 | Sondermann, H.,Soisson, S.M.,Boykevisch, S.,Yang, S.S.,Bar-Sagi, D.,Kuriyan, J. Structural analysis of autoinhibition in the ras activator son of sevenless. Cell(Cambridge,Mass.), 119:393-405, 2004 Cited by PubMed Abstract: The classical model for the activation of the nucleotide exchange factor Son of sevenless (SOS) involves its recruitment to the membrane, where it engages Ras. The recent discovery that Ras*GTP is an allosteric activator of SOS indicated that the regulation of SOS is more complex than originally envisaged. We now present crystallographic and biochemical analyses of a construct of SOS that contains the Dbl homology-pleckstrin homology (DH-PH) and catalytic domains and show that the DH-PH unit blocks the allosteric binding site for Ras and suppresses the activity of SOS. SOS is dependent on Ras binding to the allosteric site for both a lower level of activity, which is a result of Ras*GDP binding, and maximal activity, which requires Ras*GTP. The action of the DH-PH unit gates a reciprocal interaction between Ras and SOS, in which Ras converts SOS from low to high activity forms as Ras*GDP is converted to Ras*GTP by SOS. PubMed: 15507210DOI: 10.1016/j.cell.2004.10.005 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.7 Å) |
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