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

Nature Structural Biology volume 4, pages 694–699 (1997)Cite this article

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%. 1SN chemical shifts changes in the complex of RalGEF-RBD with Ras indicate an interaction similar to the intermolecular β-sheet observed for the complex between Ras and Raf-RBD.

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Authors and Affiliations

  1. Max-Planck-Institut für medizinische Forschung, Abteilung Biophysik, Jahnstraβle 29, 69120, Heidelberg, Germany

    Matthias Geyer & Hans Robert Kalbitzer

  2. Max-Planck-Institut für molekulare Physiologie, Abteilung Strukturelle Biologie, Rheinlanddamm 201, 44139, Dortmund, Germany

    Christian Herrmann, Sabine Wohlgemuth & Alfred Wittinghofer

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  1. Matthias Geyer
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Geyer, M., Herrmann, C., Wohlgemuth, S. et al. Structure of the Ras-binding domain of RalGEF and implications for Ras binding and signalling. Nat Struct Mol Biol 4, 694–699 (1997). https://doi.org/10.1038/nsb0997-694

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