Molecular basis of receptor/G-protein-coupling selectivity.
Molecular cloning studies have shown that G-protein-coupled receptors form one of the largest protein families found in nature, and it is estimated that approximately 1000 different such receptors exist in mammals. Characteristically, when activated by the appropriate ligand, an individual receptor can recognize and activate only a limited set of the many structurally closely related heterotrimeric G-proteins expressed within a cell. To understand how this selectivity is achieved at a molecular level has become the focus of an ever increasing number of laboratories. This review provides an overview of recent structural, molecular genetic, biochemical, and biophysical studies that have led to novel insights into the molecular mechanisms governing receptor-mediated G-protein activation and receptor/G-protein coupling selectivity.
Wess
J
J
Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, NIH, Bethesda, MD 20892, USA.
D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D019204:GTP-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011956:Receptors, Cell Surface / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D011956:Receptors, Cell Surface; D019204:GTP-Binding Proteins