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

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons93074

Geyer,  Matthias
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons95966

Wittinghofer,  Alfred
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons93660

Kalbitzer,  Hans Robert
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Zitation

Geyer, M., Herrmann, C., Wohlgemuth, S., Wittinghofer, A., & Kalbitzer, H. R. (1997). Structure of the Ras-binding domain of RalGEF and implications for Ras binding and signalling. Nature structural biology, 4(9), 694-699. doi:10.1038/nsb0997-694.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0024-AF7E-E
Zusammenfassung
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.