Figure 5
Comparison of Gαq residues contributing to interactions with different partners. (a) Structural regions in Gαq that can interact with its partners. Gαq is shown as a ribbon diagram colored light orange (GTPase domain) and gold (helical domain). The α3 helix and the subsequent loop are colored maroon. The P-loop is colored magenta and the three switch regions are marked as follows: Sw I, teal; Sw II, blue; and Sw III, purple. The nucleotide is shown as balls and sticks, colored green. (b) Gαq residues that substantially contribute to the interaction with RGS2 and RGS8. (c) Gαq residues that substantially contribute to the interaction with PLC-β3. (d) Gαq residues that substantially contribute to the interaction with p63RhoGEF. (e) Gαq residues that substantially contribute to the interaction with GRK2. Gαq structures (as in the complexes analyzed in Fig. 4) are depicted as gold ribbon diagrams, with partner structures omitted for clarity. Gαq residues that substantially contribute to interactions with each partner are shown as spheres and colored according to the type of energy contribution, as in Fig. 4.
