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

Nature Structural Biologyvolume 4pages694699 (1997) | Download Citation

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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%. 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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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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https://doi.org/10.1038/nsb0997-694

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