Structural and biochemical analysis of Ras-effector signaling via RalGDS
Structural and biochemical analysis of Ras-effector signaling via RalGDS
复制标题
DOI：
10.1016/s0014-5793(99)00555-4
复制
发表时间：
1999-05-21
期刊：
影响因子：
3.5
通讯作者：
Wittinghofer, A
中科院分区：
文献类型：
--
作者：
Vetter, IR;Linnemann, T;Wittinghofer, A
Ras 与其效应子 RalGDS 的 Ras 结合域 (RGS-RBD) 复合物的结构，第一个真正的 Ras 效应子复合物，已通过 X 射线晶体学解析。与 Rap-RafRBD 复合体一样（Nasser 等人，1995），相互作用是通过 Ras 开关 I 区域和 RGS-RBD 片第二链之间的蛋白质间 β 片层相互作用，但界面中相互作用的细节却截然不同。进行突变研究以研究所选界面残基对结合亲和力的贡献。凝胶过滤实验表明 Ras RGS-RBD 复合物是单体，将结果与最近使用 Ras 突变体确定的类似复合物的结构进行比较（Huang 等，1998），并讨论了部分功能丧失突变以及 Ras 与 Rap 结合的特异性。 (C) 1999 年欧洲生化学会联合会。
The structure of the complex of Ras with the Ras-binding domain of its effector RalGDS (RGS-RBD), the first genuine Ras-effector complex, has been solved by X-ray crystallography. As with the Rap-RafRBD complex (Nasser et al., 1995), the interaction is via an inter-protein beta-sheet between the switch I region of Ras and the second strand of the RGS-RBD sheet, but the details of the interactions in the interface are remarkably different. Mutational studies were performed to investigate the contribution of selected interface residues to the binding affinity. Gel filtration experiments show that the Ras RGS-RBD complex is a monomer, The results are compared to a recently determined structure of a similar complex using a Ras mutant (Huang et al., 1998) and are discussed in relation to partial loss-of-function mutations and the specificity of Ras versus Rap binding. (C) 1999 Federation of European Biochemical Societies.