Abstract
The three subtypes of human β-adrenergic receptors (β-ARs) have now been identified and fully characterized at the molecular level. The corresponding genes, two of which (β1 and β2) are devoid of introns, have been isolated and sequenced. Structurally, the β-AR proteins display the typical hallmarks of all the other membrane R7G receptors coupled to GTP binding proteins, as represented in Fig. 1. They consist of: (a) a single polypeptide chain, 350–600 residues long, with an extracellular, glycosylated, NH2-terminal domain, (b) seven hydrophobic, presumably transmembrane segments, interspersed with intra- and extracellular loops of various lengths, and (c) a COOH-terminal intracellular domain often containing several sites for phosphorylation by protein kinases (O’Dowd et al. 1989; Strosberg 1991; Strosberg and Leysen 1991).
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© 1993 Springer-Verlag Berlin Heidelberg
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Strosberg, A.D. (1993). Structure-Function Analysis of the Three β-Adrenergic Catecholamine Receptors. In: Gram, L.F., Balant, L.P., Meltzer, H.Y., Dahl, S.G. (eds) Clinical Pharmacology in Psychiatry. Psychopharmacology Series, vol 10. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-78010-3_2
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DOI: https://doi.org/10.1007/978-3-642-78010-3_2
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