2W2X
Complex of Rac2 and PLCg2 spPH Domain
2W2X の概要
エントリーDOI | 10.2210/pdb2w2x/pdb |
関連するPDBエントリー | 1DS6 2W2T 2W2V 2W2W |
分子名称 | RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 2, 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2, 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE, ... (6 entities in total) |
機能のキーワード | hydrolase, phospholipase c, phosphoinositides, rho gtpases, rac, sh2 domain, sh3 domain, signaling protein/hydrolase, signaling protein-hydrolase complex |
由来する生物種 | HOMO SAPIENS (HUMAN) 詳細 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 70181.35 |
構造登録者 | Opaleye, O.,Bunney, T.D.,Roe, S.M.,Pearl, L.H. (登録日: 2008-11-04, 公開日: 2009-05-05, 最終更新日: 2023-12-13) |
主引用文献 | Bunney, T.D.,Opaleye, O.,Roe, S.M.,Vatter, P.,Baxendale, R.W.,Walliser, C.,Everett, K.L.,Josephs, M.B.,Christow, C.,Rodrigues-Lima, F.,Gierschik, P.,Pearl, L.H.,Katan, M. Structural Insights Into Formation of an Active Signaling Complex between Rac and Phospholipase C Gamma 2. Mol.Cell, 34:223-, 2009 Cited by PubMed Abstract: Rho family GTPases are important cellular switches and control a number of physiological functions. Understanding the molecular basis of interaction of these GTPases with their effectors is crucial in understanding their functions in the cell. Here we present the crystal structure of the complex of Rac2 bound to the split pleckstrin homology (spPH) domain of phospholipase C-gamma(2) (PLCgamma(2)). Based on this structure, we illustrate distinct requirements for PLCgamma(2) activation by Rac and EGF and generate Rac effector mutants that specifically block activation of PLCgamma(2), but not the related PLCbeta(2) isoform. Furthermore, in addition to the complex, we report the crystal structures of free spPH and Rac2 bound to GDP and GTPgammaS. These structures illustrate a mechanism of conformational switches that accompany formation of signaling active complexes and highlight the role of effector binding as a common feature of Rac and Cdc42 interactions with a variety of effectors. PubMed: 19394299DOI: 10.1016/J.MOLCEL.2009.02.023 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.3 Å) |
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