Vetter, I. R. and Linnemann, T. and Wohlgemuth, S. and Geyer, M. and Kalbitzer, Hans Robert and Herrmann, C. and Wittinghofer, Alfred (1999) Structural and biochemical analysis of Ras-effector signaling via RalGDS. FEBS LETTERS, 451 (2). pp. 175-180. ISSN 1873-3468
Full text not available from this repository. (Request a copy)Abstract
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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | NUCLEOTIDE DISSOCIATION STIMULATOR; BINDING DOMAIN; H-RAS; R-RAS; PROTEIN; KINASE; IDENTIFICATION; TRANSFORMATION; ACTIVATION; INTERACTS; Ras; Ras-binding domain; structure; RalGDS; signaling |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 10 Feb 2023 11:12 |
| Last Modified: | 10 Feb 2023 11:12 |
| URI: | https://pred.uni-regensburg.de/id/eprint/49239 |
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