The structural basis of the activation of Ras by Sos

P. Ann Boriack-Sjodin, S. Mariana Margarit, Dafna Bar-Sagi and John Kuriyan
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P. Ann Boriack-Sjodin: Laboratories of Molecular Biophysics
S. Mariana Margarit: State University of New York at Stony Brook
Dafna Bar-Sagi: State University of New York at Stony Brook
John Kuriyan: Laboratories of Molecular Biophysics

Nature, 1998, vol. 394, issue 6691, 337-343

Abstract: Abstract The crystal structure of human H-Ras complexed with the Ras guanine-nucleotide-exchange-factor region of the Son of sevenless (Sos) protein has been determined at 2.8 Å resolution. The normally tight interaction of nucleotides with Ras is disrupted by Sos in two ways. First, the insertion into Ras of an α-helix from Sos results in the displacement of the Switch 1 region of Ras, opening up the nucleotide-binding site. Second, side chains presented by this helix and by a distorted conformation of the Switch 2 region of Ras alter the chemical environment of the binding site for the phosphate groups of the nucleotide and the associated magnesium ion, so that their binding is no longer favoured. Sos does not impede the binding sites for the base and the ribose of GTP or GDP, so the Ras–Sos complex adopts a structure that allows nucleotide release and rebinding.

Date: 1998
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DOI: 10.1038/28548

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