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. 2023 Jan 12;14:181. doi: 10.1038/s41467-023-35789-6

Fig. 5. Structural difference between various c-terminal mutants of p110α compared to WT p110α/p85α, and mapping of the p110α membrane binding interface.

Fig. 5

A–C HDX comparing p110α/p85α WT vs H1047R (A), G1049R (B) and ΔCter (1–1048) (C). Significant differences in deuterium exchange are mapped on to the structure of p110α/p85α H1047R according to the legend (PDB: 3HHM] (A + B) and 4OVU (C)). The graph of the sum of number of deuteron difference in deuterium incorporation for p110α in each experiment is shown below, with each point representing a single peptide. Peptides coloured in red are those that had a significant change in the mutants (>0.4 Da and 5% difference at any timepoint, with a two-tailed t-test p < 0.01). Error bars are shown as the sum of S.D. across all time points. (n = 3 for each time point). D, E HDX comparing p110α/p85α WT vs M1043L (D) and N1068fs (E). The graph of the #D difference in deuterium incorporation for p110α in each experiment is shown below, with each point representing a single peptide. Error bars are shown as the sum of S.D. across all time points (n = 3 for each time point). For all panels, the HDX-MS data for p85 subunits is shown in Supplementary Fig. 5, along with representative peptides showing significant changes. The full HDX-MS data is available in the source data.