Spoerner, M. and Prisner, T. F. and Bennati, M. and Hertel, M. M. and Weiden, N. and Schweins, T. and Kalbitzer, Hans Robert (2005) Conformational states of human H-ras detected by high-field EPR, ENDOR, and P-31 NMR spectroscopy. MAGNETIC RESONANCE IN CHEMISTRY, 43. S74-S83. ISSN 0749-1581, 1097-458X
Full text not available from this repository. (Request a copy)Abstract
Ras is a central constituent of the intracellular signal transduction that switches between its inactive state with GDP bound and its active state with GTP bound. A number of different X-ray structures are available. Different magnetic resonance techniques were used to characterise the conformational states of the protein and are summarised here. P-31 NMR spectroscopy was used as probe for the environment of the phosphate groups of the bound nucleotide. It shows that in liquid solution additional conformational states in the GDP as well as in the GTP forms coexist which are not detected by X-ray crystallography. Some of them can also be detected by solid-state NMR in the micro crystalline state. EPR and ENDOR spectroscopy were used to probe the environment of the divalent metal ion (Mg2+ was replaced by Mn2+) bound to the nucleotide in the protein. Here again different states could be observed. Substitution of normal water by O-17-enriched water allowed the determination of the number of water molecules in the first coordination sphere of the metal ion. In liquid solution, they indicate again the existence of different conformational. states. At low temperatures in the frozen state ENDOR spectroscopy suggests that only one state exists for the GDP- and GTP-bound form of Ras, respectively. Copyright (c) 2005 John Wiley & Sons, Ltd.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ELECTRON-PARAMAGNETIC-RESONANCE; ENVELOPE MODULATION SPECTROSCOPY; GTP-BINDING PROTEINS; P21 RAS; TRIPHOSPHATE CONFORMATION; SIGNAL-TRANSDUCTION; MOLECULAR SWITCH; HYDROLYSIS; GDP; P21(RAS); EPR; ENDOR; P-31 NMR; Ras; conformational states |
| 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: | 23 Apr 2021 12:24 |
| Last Modified: | 23 Apr 2021 12:24 |
| URI: | https://pred.uni-regensburg.de/id/eprint/35484 |
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