| Item type: | Article | ||||||||||||||||||||||||||||
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| Journal or Publication Title: | Journal of molecular biology | ||||||||||||||||||||||||||||
| Publisher: | ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD | ||||||||||||||||||||||||||||
| Place of Publication: | LONDON | ||||||||||||||||||||||||||||
| Volume: | 342 | ||||||||||||||||||||||||||||
| Number of Issue or Book Chapter: | 3 | ||||||||||||||||||||||||||||
| Page Range: | pp. 1033-1040 | ||||||||||||||||||||||||||||
| Date: | 2004 | ||||||||||||||||||||||||||||
| Institutions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Alumni or Retired > Prof. Dr. Eike Brunner Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer | ||||||||||||||||||||||||||||
| Identification Number: |
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| Classification: |
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| Keywords: | PHOSPHORYLATED AMINO-ACIDS; ROTATING SOLIDS; CHEMICAL-SHIFTS; P21; PHOSPHATES; RESOLUTION; RESONANCE; EXCHANGE; SYSTEMS; SPECTRA; Ras protein; effector loop mutants; molecular switches; phosphorous solid-state NMR spectroscopy | ||||||||||||||||||||||||||||
| Dewey Decimal Classification: | 500 Science > 570 Life sciences | ||||||||||||||||||||||||||||
| Status: | Published | ||||||||||||||||||||||||||||
| Refereed: | Unknown | ||||||||||||||||||||||||||||
| Created at the University of Regensburg: | Unknown | ||||||||||||||||||||||||||||
| Item ID: | 16610 |
Web of ScienceAbstract
Cycling between a GTP bound "on" state and a GDP bound "off" state, guanine nucleotide-binding (GNB) proteins act as molecular switches. The switching process and the interaction with effectors, GTPase-activating proteins, and guanosine nucleotide-exchange factors is accompanied by pronounced conformational changes of the switch regions of the GNB proteins. The aim of the present contribution is ...
Abstract
Cycling between a GTP bound "on" state and a GDP bound "off" state, guanine nucleotide-binding (GNB) proteins act as molecular switches. The switching process and the interaction with effectors, GTPase-activating proteins, and guanosine nucleotide-exchange factors is accompanied by pronounced conformational changes of the switch regions of the GNB proteins. The aim of the present contribution is to correlate conformational changes observed by liquid-state NMR with solid-state P-31 NMR data and with the results of X-ray crystallography. Crystalline wild-type Ras complexed with GTP analogs such as GppCH(2)p and GppNHp could be prepared. At low temperatures, two different signals were found for the gamma-phosphate group of GppNHp bound to wild-type Ras. This behavior indicates the existence of two different conformations of the molecule in the crystalline state as it is found in solution but not by X-ray crystallography. In contrast to the GppNHp complex, the two separate gamma-phosphate signals could not be observed for GppCH2p bound to wild-type Ras. However, an increasing linewidth at low temperature indicates the presence of an exchange process. The results obtained for the wild-type protein are compared with the behavior of GppNHp complexes of the effector loop mutants Ras(T35S) and Ras(T35A). These mutants prefer a conformation similar to the GDP bound "off" state. (C) 2004 Elsevier Ltd. All rights reserved.
Metadata last modified: 29 Sep 2021 07:38
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