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. 2017 Apr 28;8:15061. doi: 10.1038/ncomms15061

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Copyright © 2017, The Author(s)

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(a) SOS^FL(W729E) and SOS^HDPC(W729E), SOS mutants that are impaired in allosteric Ras binding, show a very low level of membrane binding compared with wild-type SOS. (b) The allosteric site of SOS^CatPR is autoinhibited by the PR domain and shows a lower binding affinity to Ras^(Y64A) than SOS^Cat. Ras^(Y64A) exclusively binds to the allosteric site. Linear fits were applied with the y intercept to be zero. (c) Relative binding frequency of 1 nM SOS^FL at different concentrations of recombinant Grb2. Lipid composition (in mol%): egg-PC/MCC-DOPE/DOPS=94/3/3. Surface density of Ras: ∼1,200 μm⁻².