G protein-coupled receptor kinases (GRKs) selectively recognize activated G protein-coupled receptors (GPCRs) through an allosteric receptor docking site. Until recently, the molecular basis for how receptor docking leads to GRK activation was poorly understood. Biochemical and structural evidence now suggests that a short N-terminal region of the GRK forms the primary interaction site for GPCRs. Upon docking to the receptor, the N-terminal region forms an .dgcir; helix that binds to the kinase domain and stabilizes it in a closed, active conformation, thereby providing a direct link between receptor recognition and stimulation of kinase activity.