Fig. 7.

Conformational changes in GRK2 upon ligand binding. Electron density is shown for a 3σ |F_o| − |F_c| omit map of the GRK2-CMPD103A-Gβγ structure. Positive and negative density is shown in green and red, respectively. Residues from the apoGRK2-Gβγ structure are colored slate, and residues from the GRK2-CMPD103A-Gβγ structure are colored green. The labeled residues correspond to the mutation from bovine GRK2 to human GRK1 (red). A, nonconserved residues in the P-loop and hinge region undergo small conformational changes upon inhibitor binding. B, displacement of Leu235 by the D ring of CMPD103A.