Mutagenesis of the Human 5-HT_1B Receptor: Differences from the Closely Related 5-HT_1A Receptor and the Role of Residue F331 in Signal Transduction

References

• Kobilka B., Kobilka T., Daniel K., Regan J., Caron M., Lefkowitz R. Chimeric alpha 2-, beta 2-adrenergic receptors: delineation of domains involved in effector coupling and ligand binding specificity. Science 1988; 240: 1310–1316
   PubMed Web of Science ®Google Scholar
• Strader C., Sigal I., Dixon R. Structural basis of β-adrenergic receptor function. FASEB J. 1989; 7: 1825–1832
   Google Scholar
• Lefkowitz R. J., Coteccia S., Samama P., Costa T. Constitutive activity of receptors coupled to guanine nucleotide regulatory proteins, Trends Pharmacol. Sci. 1993; 14: 303–307
   Google Scholar
• Strader C. D., Fong T. M., Graziano M. P., Tota M. R. The family of G-protein-coupled receptors. FASEB J 1995; 9: 745–754
   PubMed Web of Science ®Google Scholar
• Hamblin M. W., Metcalf M. A. Primary structure and functional characterization of a human 5-HT1D-type serotonin receptor. Mol. Pharmacol. 1991; 40: 143–148
   PubMed Web of Science ®Google Scholar
• Boschert U., Amara D. A., Segu L., Hen R. The mouse 5-hydroxytryptamine1Breceptor is localized predominantly on axon terminals. Neuroscience 1994; 58: 167–182
   PubMedGoogle Scholar
• Demchyshyn L., Sunahara R. K., Miller K., Teitler M., Hoffman B. J., Kennedy J. L., Seeman P., Van Tol H. H.M., Niznik H. B. A human serotonin1Dreceptor variant (5HT1Dβ) encoded by an intronless gene on chromosome 6. Proc. Natl Acad. Sci. U.S.A. 1992; 89: 5522–5526
   PubMed Web of Science ®Google Scholar
• Nordvall G., Hacksell U. Binding-site modeling of the muscarinic m1receptor – a combination of homology-based and indirect approaches. J. Med. Chem. 1993; 36: 967–976
   PubMedGoogle Scholar
• Henderson R., Baldwin J. M., Ceska T. A., Zemlin F., Beckmann E., Downing K. H. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol 1990; 213: 899–929
   PubMed Web of Science ®Google Scholar
• Fong T. M., Strader C. D. Functional mapping of the ligand binding sites of G-protein coupled receptors. Med. Res. Rev. 1994; 14: 387–399
   Google Scholar
• Deng W. P., Nickoloff J. A. Site-directed mutagenesis of virtually any plasmid by eliminating a unique site. Anal. Biochem. 1992; 200: 81–88
   PubMed Web of Science ®Google Scholar
• Felgner P., Gadek T., Holm M., Roman R., Chan H., Wenz M., Northrop J., Ringold G., Danielsen M. Lipofection: a highly efficient, lipidmediated DNA-transfection procedure. Proc. Natl Acad. Sci. U.S.A. 1987; 84: 7413–7417
   PubMed Web of Science ®Google Scholar
• Markwell M. A.K., Haas S. M., Bieber L. L., Tolbert N. E. A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal. Biochem. 1978; 87: 206–210
   PubMed Web of Science ®Google Scholar
• Woodward R., Daniell S. J., Strange P. G., Naylor L. H. Structural studies on dopamine D2 receptors – mutation of a histidine residue specifically affects the binding of a subgroup of substituted benzamide drugs. J. Neurochem 1994; 62: 1664–1669
   Google Scholar
• Hibert M. F., Trumpp K. S., Bruinvels A., Hoflack J. Three-dimensional models of cationic neurotransmitter G-protein coupled receptors. Mol. Pharmacol. 1991; 40: 8–15
   PubMed Web of Science ®Google Scholar
• Ho B. Y., Karschin A., Branchek T., Davidson N., Lester H. A. The role of conserved aspartate and serine residues in ligand binding and in function of the 5-HT1Areceptor: a site-directed mutation study. FEBS Lett. 1992; 312: 259–262
   PubMedGoogle Scholar
• Strader C., Candelore M., Hill W., Sigal I., Dixon R. Identification of two serine residues involved in agonist activation of the β-adrenergic receptor. J. Biol. Chem 1989; 264: 13572–13578
   PubMedGoogle Scholar
• Pollock N. J., Manelli A. M., Hutchins C. W., Steffey M. E., Mackenzie R. G., Frail D. E. Serine mutations in transmembrane V of the dopamine D1receptor affect ligand interactions and receptor activation. J. Biol. Chem. 1992; 267: 17780–17786
   PubMed Web of Science ®Google Scholar
• Cox B. A., Henningsen R. A., Spanoyannis A., Neve R. L., Neve K. A. Contributions of conserved serine residues to the interactions of ligands with dopamine D2receptors. J. Neurochem. 1992; 59: 627–635
   Google Scholar
• Mansour A., Meng F., Meador-Woodruff J. H., Taylor L. P., Civelli O., Akil H. Site-directed mutagenesis of the human dopamine D2receptor. Eur. J. Pharmacol. 1992; 227: 205–214
   PubMed Web of Science ®Google Scholar
• Choudhary M. S., Craigo S., Roth B. L. A single point mutation (Phe340→Leu340) of a conserved phenylalanine abolishes 4-[125I]iodo-(2,5-dimethoxy)phenylisopropylamine and [3H]mesulergine but not [3H]ketanserin binding to 5-hydroxytryptamine2receptors. Mol. Pharmacol. 1993; 43: 755–761
   PubMed Web of Science ®Google Scholar
• Roth B. L., Choudhary M. S., Khan N., Uluer A. High-affinity binding is not sufficient for agonist efficacy at 5-hydroxytryptamine2Areceptors: evidence in favor of a modified ternary complex model. J. Pharmacol. Exp. Ther. 1997; 280: 576–583
   PubMed Web of Science ®Google Scholar
• Cho W., Taylor L. P., Mansour A., Akil H. Hydrophobic residues of the D2dopamine receptor are important for binding and signal transduction. J. Neurochem. 1995; 65: 2105–2115
   Google Scholar
• Dixon R. A.F., Sigal I. S., Strader C. D. Structure-function analysis of the β-adrenergic receptor, Cold Spring Harbor Symp. Quant. Biol. 1988; 53: 487–497
   PubMedGoogle Scholar
• Samama P., Coteccia S., Costa T., Lefkowitz R. J. A mutational-induced activated state of the β2-adrenergic receptor. J. Biol. Chem. 1993; 268: 4625–4636
   PubMed Web of Science ®Google Scholar
• Tiberi M., Caron M. G. High agonist-independent activity is a distinguishing feature of the dopamine D1Breceptor subtype. J. Biol. Chem. 1994; 269: 27925–27931
   PubMed Web of Science ®Google Scholar
• Kjelsberg M. A., Cotecchia S., Ostrowski J., Caron M. G., Lefkowitz R. J. Constitutive activation of the α1B-adrenergic receptor by all amino acid substitutions at a single site. J. Biol. Chem. 1992; 267: 1430–1433
   PubMed Web of Science ®Google Scholar
• Thomas D. R., Faruq S. A., Balcarek J. M., Brown A. M. Pharmacological characterisation of [35S]-GTPγS binding to chinese hamster ovary cell membranes stably expressing cloned human 5-HT1Dreceptor subtypes. J. Receptor Signal Transduct. Res. 1995; 15: 199–211
   PubMed Web of Science ®Google Scholar