The emergence of Biotechnology has provided pharmacologists with a variety of methods for investigating the structure, the function, and the regulation of membrane-bound receptors with a precision that was not imagined even five years ago. These new tools have been developed and used to analyze the known catecholamine beta 1- and beta 2-adrenergic receptors and to discover and study a new subtype, the beta 3 receptor. We review here the salient features of each of these three receptors, compare their structural and functional properties, and propose models to explain their differential regulation in time and space. A whole family of proteins has now been found to share with the beta-adrenergic receptors their most prominent features, including seven transmembrane domains and coupling with GTP-binding "G" proteins. We therefore propose that the biotechnology-based procedures developed for the beta-adrenergic receptors will be well applicable to the other members of this "R7G" family of receptors.