Agonist-bound G-protein-coupled receptors (GPCRs) facilitate GDP-GTP exchange on their cognate G proteins. The binding properties of GPCRs are adequately described by the ternary complex model. However, in this article a more realistic (steady-state) model, which is necessary to describe the catalytic effect of agonist-bound receptors on G-protein activation, will be discussed. This model predicts that agonist potency and efficacy might vary from tissue to tissue, depending on the G-protein concentration and can be extended to explain why an agonist's ability to increase the receptor's affinity for empty G proteins (in the absence of GTP) is related to the agonist's efficacy.