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. 2015 Feb 9;290(14):9037–9049. doi: 10.1074/jbc.M114.634329

FIGURE 5.

FIGURE 5.

Binding of Gαi1-GDP stabilizes the GPR motif and induces allosteric stabilization of other regions within RGS14. A, differential HDX heat map for the RGS14·Gαi1-GDP complex. Each bar represents an individual peptide with the color corresponding to the average percentage change in deuterium exchange between apo-RGS14 and RGS14·Gαi1 over six time points (10, 30, 60, 300, 900, and 3,600 s). The numbers in the first parentheses indicate the S.D. value for three replicates. The numbers in the second parentheses indicate the charge of the peptide. Residues corresponding to the RGS domain, RBDs, and GPR motif are boxed in black. Changes in deuterium exchange are indicated by the colored scale bar. B, average percentage change in deuterium exchange for the RGS14·Gαi1 complex mapped onto the crystal structure of human RGS10 bound to AlF4−-activated Gαi3 (PDB ID: 2IHB). Gαi3 is represented in purple. Differences in the percentage of deuterium exchange are indicated by the colored scale bar.