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2WM9

Structure of the complex between DOCK9 and Cdc42.

2WM9 の概要
エントリーDOI10.2210/pdb2wm9/pdb
関連するPDBエントリー1A4R 1AJE 1AM4 1AN0 1CEE 1CF4 1DOA 1E0A 1EES 1GRN 1GZS 1KI1 1KZ7 1KZG 1NF3 1WG7 2ASE 2DFK 2NGR 2WMN 2WMO
分子名称DEDICATOR OF CYTOKINESIS PROTEIN 9, CELL DIVISION CONTROL PROTEIN 42 HOMOLOG, GLYCEROL, ... (4 entities in total)
機能のキーワードpolymorphism, cell membrane, phosphoprotein, nucleotide-binding, alternative splicing, guanine-nucleotide releasing factor, cell cycle, methylation, lipoprotein, coiled coil, gtp-binding, gefs, dock9, cdc42, prenylation
由来する生物種HOMO SAPIENS (HUMAN)
詳細
タンパク質・核酸の鎖数2
化学式量合計71479.96
構造登録者
Yang, J.,Roe, S.M.,Barford, D. (登録日: 2009-06-30, 公開日: 2009-09-22, 最終更新日: 2024-05-08)
主引用文献Yang, J.,Zhang, Z.,Roe, S.M.,Marshall, C.J.,Barford, D.
Activation of Rho Gtpases by Dock Exchange Factors is Mediated by a Nucleotide Sensor.
Science, 325:1398-, 2009
Cited by
PubMed Abstract: Activation of Rho guanosine triphosphatases (GTPases) to the guanine triphosphate (GTP)-bound state is a critical event in their regulation of the cytoskeleton and cell signaling. Members of the DOCK family of guanine nucleotide exchange factors (GEFs) are important activators of Rho GTPases, but the mechanism of activation by their catalytic DHR2 domain is unknown. Through structural analysis of DOCK9-Cdc42 complexes, we identify a nucleotide sensor within the alpha10 helix of the DHR2 domain that contributes to release of guanine diphosphate (GDP) and then to discharge of the activated GTP-bound Cdc42. Magnesium exclusion, a critical factor in promoting GDP release, is mediated by a conserved valine residue within this sensor, whereas binding of GTP-Mg2+ to the nucleotide-free complex results in magnesium-inducing displacement of the sensor to stimulate discharge of Cdc42-GTP. These studies identify an unusual mechanism of GDP release and define the complete GEF catalytic cycle from GDP dissociation followed by GTP binding and discharge of the activated GTPase.
PubMed: 19745154
DOI: 10.1126/SCIENCE.1174468
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.2 Å)
構造検証レポート
Validation report summary of 2wm9
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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