Spoerner, Michael and Wittinghofer, Alfred and Kalbitzer, Hans Robert (2004) Perturbation of the conformational equilibria in Ras by selective mutations as studied by P-31 NMR spectroscopy. FEBS LETTERS, 578 (3). pp. 305-310. ISSN 0014-5793,
Full text not available from this repository. (Request a copy)Abstract
Ras regulates a variety of different signal transduction pathways acting as molecular switch. It was shown by liquid and solid-state P-31 NMR spectroscopy that Ras exists in the guanosine-5'-(beta, gamma-imido)triphosphate bound form in at least two conformational states interconverting in millisecond time scale. The relative population between the two conformational states affects drastically the affinity of Ras to its effectors. P-31 NMR spectroscopy shows that the conformational equilibrium can be shifted specifically by point mutations, including mutations with oncogenic potential, thus modifying the effector interactions and their coupling to dynamic properties of the protein. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | BINDING DOMAIN; PROTEIN-KINASE; P21(RAS); P21; Ras; conformational dynamics; effector interaction; P-31 NMR spectroscopy |
| 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: | 21 Jun 2021 08:24 |
| Last Modified: | 21 Jun 2021 08:24 |
| URI: | https://pred.uni-regensburg.de/id/eprint/36866 |
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