Go to content
UR Home

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

Geyer, M. and Herrmann, C. and Wohlgemuth, S. and 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.

Full text not available from this repository.

at PubMed


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.

Export bibliographical data

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
Deposited on:13 Sep 2010 08:14
Last modified:13 Sep 2010 08:14
Item ID:16552
Owner only: item control page
  1. Homepage UR

University Library

Publication Server


Publishing: oa@ur.de

Dissertations: dissertationen@ur.de

Research data: daten@ur.de

Contact persons