Figure 6
Multi-specificity analysis of Gαq. (a) Gαq residues that substantially contribute to interactions with its partners, classified according to the number of binding partners interacting with each residue, colored as in the key. Gαq is shown as a gold ribbon. The contributions of RGS2 and RGS8 residues were combined into a consensus map representing both RGS proteins. (b) Gαq residues that uniquely contribute to interactions with only one partner (i.e. those marked with yellow spheres in panel a), shown as spheres and colored according to the identity of the partner with which they interact: p63RhoGEF, orange; PLC-β3, yellow; RGS2/8, cyan; GRK2, light blue. (c) Gαq residues that interact uniquely with GAPs (PLC-β3/RGS proteins) as opposed to non-GAPs (p63RhoGEF/GRK2). Gαq residues that contribute to interactions with these partners are shown as spheres and colored as follows: residues that contribute to interactions with p63RhoGEF and/or GRK2 (contributions to “effectors” only) are colored purple, residues that contribute to interactions with PLC-β3 and/or RGS2/8 (contributions to “GAPs” only) are colored green, and residues that contribute to interactions with both effectors and GAPs are colored teal. (d) Gαq residues that interact with particular effector combinations. Contributing Gαq residues are shown as spheres and colored as follows: residues that contribute to interactions with all three effectors (p63RhoGEF, GRK2, and PLC-β3) are colored lilac, residues that contribute to interactions with PLC-β3 and with RGS2/8 are colored green, residues that contribute to interactions with PLC-β3 only are colored yellow, residues that contribute to interactions with only p63RhoGEF are colored orange, residues that contribute to interactions with only RGS2/8 are colored cyan and residues that contribute to interactions with all four partners are colored maroon.
