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Structure of the Ras-binding domain of RalGEF and implications for Ras binding and signalling

Geyer, M., Herrmann, C., Wohlgemuth, S., Wittinghofer, A. and Kalbitzer, Hans Robert (1997) Structure of the Ras-binding domain of RalGEF and implications for Ras binding and signalling. Nature structural biology 4 (9), pp. 694-699.

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The solution structure of the Ras-binding domain (RBD) of Ral guanine-nucleotide exchange factor RalGEF was solved by NMR spectroscopy. The overall structure is similar to that of Raf-RBD, another effector of Ras, although the sequence identity is only 13%. 15N chemical shifts changes in the complex of RalGEF-RBD with Ras indicate an interaction similar to the intermolecular beta-sheet observed for the complex between Ras and Raf-RBD.

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Item type:Article
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
9302994PubMed ID
Amino Acid SequenceMESH
Binding SitesMESH
GTP-Binding Proteins/chemistryMESH
Magnetic Resonance SpectroscopyMESH
Models, MolecularMESH
Molecular Sequence DataMESH
Signal Transduction/physiologyMESH
rap GTP-Binding ProteinsMESH
ras Proteins/chemistryMESH
Dewey Decimal Classification:500 Science > 570 Life sciences
Created at the University of Regensburg:Unknown
Item ID:16552
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