Interrogating 7TM receptors: Does texture in the question yield greater texture in the answer?

References

• Liu J, Perumal NB, Oldfield CJ, Su EW, Uversky VN, Dunker AK. Intrinsic order in transcription factors. Biochemistry 2006;45:6873–88.
   PubMed Web of Science ®Google Scholar
• Hilser VJ, Thompson EB. Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins. Proc Natl Acad Sci USA 2007;104:8311–5.
   PubMed Web of Science ®Google Scholar
• Fraunfelder H, Parak F, Young RD. Conformational substrates in proteins. Annu Rev Biophys Biophys Chem 1988;17:451–79.
   PubMedGoogle Scholar
• Fraunfelder H, Sligar SG, Wolynes PG. The energy landscapes and motions of proteins. Science 1991;254:1598–603.
   PubMed Web of Science ®Google Scholar
• Hilser VJ, Garcia-Moreno B, Oas TG, Kapp G, Whitten ST. A statistical thermodynamic model of the protein ensemble. Chem Rev 2006;106:1545–58.
   PubMed Web of Science ®Google Scholar
• Onaran HO, Costa T. Agonist efficacy and allosteric models of receptor action. Ann N Y Acad Sci 1997;812:98–115.
   PubMed Web of Science ®Google Scholar
• Onaran HO, Scheer A, Cotecchia S, Costa T. A look at receptor efficacy. From the signaling network of the cell to the intramolecular motion of the receptor. In: Kenakin TP, Angus JA, eds. The Pharmacology of Functional, Biochemical, and Recombinant Systems Handbook of Experimental Pharmacology. Germany: Springer, Heidelberg, 2000;148:217–80.
   Google Scholar
• Burgen ASV. Conformational changes and drug action. Fed Proc 1966;40:2723–8.
   Google Scholar
• Kjelsberg MA, Cottechia S, Ostrowski J, Caron MG, Lefkowitz RJ. Constitutive activation of the α1B-adrenergic receptor by all amino acid substitutions at a single site. J Biol Chem 1992;267:1430–3.
   PubMed Web of Science ®Google Scholar
• Gether U, Lin S, Kobilka BK.Fluorescent labeling of purified β2-adrenergic receptor: evidence for ligand specific conformational changes. J Biol Chem 1995;270:28268–75.
   PubMed Web of Science ®Google Scholar
• Ghanouni P, Gryczynski Z, Steenhuis JJ, Lee TW, Farrens DL, Lakowicz JR, Kobilka BK. Functionally different agonists produce distinct conformations in G-protein coupling domains of the β2-adrenergic receptor. J Biol Chem 2001;276:24433–6.
   PubMed Web of Science ®Google Scholar
• Hruby VJ, Tollin G. Plasmon-waveguide resonance (PWR) spectroscopy for directly viewing rates of GPCR/G-protein interactions and quantifying affinities. Curr. Opin Pharmacol. 2007;7:507–14.
   Google Scholar
• Swaminath G, Xiang Y, Lee TW, Steenhuis J, Parnot C, Kobilka BK. Sequential Binding of agonists to the β2-adrenoceptor: B2 kinetic evidence for intermediate conformation states. J Biol Chem 2004;279:686–91.
   PubMed Web of Science ®Google Scholar
• Palanche T, Ilien B, Zoffmann S, Reck MP, Nucher B, Edelstein SJ, et al. The Neurokinin A receptor activates calcium and cAMP responses through distinct conformational states. J Biol Chem 2001;276:34853–61.
   Web of Science ®Google Scholar
• Ikezu T, Okamoto T, Ogata E, Nishimoto I. Amino acid 356-372 constitute a Gi-activator sequence of the α2-adrenergic receptor and have a Phe substitute in the G-protein-activator sequence motif. FEBS Lett 1992;311:29–32.
   PubMed Web of Science ®Google Scholar
• Zuscik MJ, Porter JE, Gaivin R, Perez DM. Identification of a conserved switch residue responsible for selective constitutive activation of the beta2-adrenergic receptor. J Biol Chem 1998;273:3401–7.
   PubMed Web of Science ®Google Scholar
• Roth BL, Chuang D-M. Multiple mechanisms of serotonergic signal transduction. Life Sci 1987;41:1051–64.
   PubMed Web of Science ®Google Scholar
• Lawler CP, Prioleau CM, Lewis MM, Mak C, Jiang D, Schetz JA, Gonzalez AM, Sibley DR, Mailman RB. Interactions of the novel antipsychotic aripiprazole (OPC-14597) with dopamine and serotonin receptor subtypes Neuropsychopharmacology 1996;20:612–62.
   Google Scholar
• Ward JS, Merrit L, Calligaro DO, Bymaster FP, Shannon HE, Sawyer BD, Mitch CH, Deeter JB, Peters SC, Sheardown MJ, Olesen PH, Swedberg MDB, Sauerberg P. Functionally selective M1 muscarinic agonists. 3. Side chains and azacycles contributing to functional muscarinic selectivity among pyrazacycles. J Med Chem 1995;38:3469–81.
   Google Scholar
• Heldman E, Barg J, Fisher A, Levy R, Pittel Z, Zimlichman R, Kushnir M, Vogel Z. Pharmacological basis for functional selectivity of partial muscarinic receptor agonists. Eur J Pharmacol 1996;297:283–91.
   Google Scholar
• Kenakin TP, Morgan PH. The theoretical effects of single and multiple transducer receptor coupling proteins on estimates of the relative potency of agonists. Mol Pharmacol 1989;35:214–22.
   PubMed Web of Science ®Google Scholar
• Kenakin TP. Agonist-receptor efficacy II: Agonist trafficking of receptor signals. Trends Pharmacol Sci 1995;16:232–8.
   PubMed Web of Science ®Google Scholar
• Gray JA, Roth BL. Paradoxical trafficking and regulation of 5-HT2A receptors by agonists and antagonists. Brain Res Bull 2001;56:441–51.
   PubMed Web of Science ®Google Scholar
• Roettger BF, Ghanekar D, Rao R, Toledo C, Yingling J, Pinon D, Miller LJ. Antagonist-stimulated internalization of the G protein-coupled cholecystokinin receptor. Mol Pharmacol 1997;51:357–62.
   PubMed Web of Science ®Google Scholar
• Kenakin TP. Ligand-selective receptor conformations revisited: The promise and the problem. Trends Pharmacol Sci 2003;24:346–54.
   PubMed Web of Science ®Google Scholar
• Bouvier M. Oligomerization of G-protein-coupled transmitter receptors Nat Rev Neurosci 2001;2:274–86.
   PubMed Web of Science ®Google Scholar
• Persani L, Calebiro D, Bonomi M. Technology insight: Modern methods to monitor protein-protein interactions reveal functional TSH receptor oligomerization. Nat Clin Pract Endocrinol Metab 2007;3:180–90.
   Google Scholar
• Pfleger KDG, Eidne KA. Illuminating insights into protein-protein interactions using bioluminescence resonance energy transfer (BRET). Nat Methods 2006;3:165–74.
   PubMed Web of Science ®Google Scholar
• Li IT, Pham E, Truong K. Protein biosensors based on the principle of fluorescence resonance energy transfer for monitoring cellular dynamics Biotechnol Lett 2006;28:1971–82.
   Google Scholar
• Giepmans BNG, Adams SR, Ellisman MH, Tsien RY. Review—The fluorescent toolbox for assessing protein location and function. Science 2006;312:217–24.
   PubMed Web of Science ®Google Scholar
• Kenakin TP. New concepts in drug discovery: Collateral efficacy and permissive antagonism. Nat Rev Drug Discov 2005;4:919–27.
   PubMed Web of Science ®Google Scholar
• Mukhopadhyay S, Howlett AC. Chemically distinct ligands promote differential CB1 cannabinoid receptor-Gi protein interactions. Mol Pharmacol 2005;67:2016–24.
   PubMed Web of Science ®Google Scholar
• Kenakin TP. Collateral efficacy in drug discovery: Taking advantage of the good (allosteric) nature of 7TM receptors. Trends Pharmacol Sci 2007;28:407 –15.
   PubMed Web of Science ®Google Scholar
• Urban JD, Clarke WP, Zastrow M, Nichols DE, Kobilka B, Weinstein H, et al. Functional selectivity and classical concepts of quantitative pharmacology. J Pharmacol Exp Ther 2007;320:1 –13.
   PubMed Web of Science ®Google Scholar
• Hermans E. Biochemical and pharmacological control of the multiplicity of coupling at G-protein receptors. Pharmacol Ther 2003;99:25–44.
   PubMed Web of Science ®Google Scholar
• Perez DM, Karnick SS. Multiple signaling states of G-protein coupled receptors Pharmacol Rev 2005;57:147 –61.
   PubMed Web of Science ®Google Scholar
• Kukkonen JP. Regulation of receptor-coupling to (multiple) G proteins: A challenge for basic research and drug discovery. Receptors Channels 2004;10: 167–83.
   PubMedGoogle Scholar
• Watson C, Chen G, Irving PE, Way J, Chen W-J, Kenakin TP. The use of stimulus-biased assay systems to detect agonist-specific receptor active states: Implications for the trafficking of receptor stimulus by agonists. Mol Pharmacol 2000;58:1230–8.
   PubMed Web of Science ®Google Scholar
• Maillet EL, Pellegrini N, Valant C, Bucher B, Hibert M, Bourguignon J-J, Galzi J-L. A novel, conformation-specific allosteric inhibitor of the tachykinin NK2 receptor (NK2R) with functionally selective properties. FASEB J 2007;21:2124–34.
   PubMed Web of Science ®Google Scholar
• Mathiesen JM, Ulven T, Martini L, Gerlach LO, Heineman A, Kostenis E. Identification of indole derivatives exclusively interfering with a G protein-independent signaling pathway of the prostaglandin D2 receptor CRTH2. Mol Pharmacol 2005;68:393–402.
   PubMed Web of Science ®Google Scholar
• Maeda K, Nakata H, Koh Y, Miyakawa T, Ogata H, Takaoka Y, Sbibayama S, Sagawa K, Fukushima D, Moravek J, Koyanagi Y, Mitsuya H. Spirodiketopiperazine-based CCR5 inhibitor which preserves CC-chemokine/CCR5 interactions and exerts potent activity against R5 human immunodeficiency virus type 1 in vitro. J Virol 2004;78:8654–62.
   PubMed Web of Science ®Google Scholar
• Watson C, Jenkinson S, Kazmierski W, Kenakin TP. The CCR5 Receptor-based mechanism of action of 873140, a potent allosteric non-competitive HIV entry-inhibitor. Mol Pharmacol 2005;67:1268–82.
   PubMed Web of Science ®Google Scholar
• Rees S, Morrow D, Kenakin TP. GPCR drug discovery through the exploitation of allosteric drug binding sites. Receptors Channels 2002;8:261–8.
   PubMedGoogle Scholar
• Hay DL, Christopoulos G, Christopoulos A, Sexton PM. Amylin receptors: Molecular composition and pharmacology. Biochem Soc Trans. 2004;32(Part 5):865–7.
   Google Scholar
• Udawela M, Christopoulos G, Tilakaratne N, Christopoulos A, Albiston A, Sexton PM. Distinct receptor activity-modifying protein domains differentially modulate interaction with calcitonin receptors. Mol Pharmacol 2006;69(6):1984–9.
   Google Scholar
• Hay DL, Poyner DR, Sexton PM. GPCR modulation by RAMPS. Pharmacol Therapeutics 2006;109(1-2):173–97.
   PubMed Web of Science ®Google Scholar
• McGuinness R. Impedance-based cellular assay technologies: recent advances, future promise. Curr Opin Pharmacol 2007;7:535–40.
   PubMed Web of Science ®Google Scholar
• Fang Y. Label-free cell-based assays with optical biosensors in drug discovery ASSAY. Drug Dev Technol 2006;4:583–95.
   PubMed Web of Science ®Google Scholar
• Azzi M, Charest PG, Angers S, Rousseau G, Kohout T, Bouvier M. β-arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G-protein-coupled receptors. Proc Natl Acad Sci USA 2003;100:11406–11.
   PubMed Web of Science ®Google Scholar
• Baker JG, Hall IP, Hill SJ. Agonist and inverse agonist actions of β-blockers at the human β2-adrenoceptor provide evidence for agonist-directed signaling. Mol Pharmacol 2003;64:1357–69.
   PubMed Web of Science ®Google Scholar
• Galandrin S, Bouvier M. Distinct signaling profiles of β1 and β2 adrenergic receptor ligands toward adenylyl cyclase and mitogen-activated protein kinase reveals the pluridimensionality of efficacy. Mol Pharmacol 2006;70:1575–84.
   PubMed Web of Science ®Google Scholar
• Lefkowitz RJ. Historical review: A brief history and personal retrospective of seven-transmembrane receptors. Trends Pharmacol Sci 2004;25(8):413–22.
   Google Scholar
• Lefkowitz RJ, Shenoy SK. Transduction of receptor signals by β-arrestins. Science 2005;308:512–7.
   PubMed Web of Science ®Google Scholar
• Lefkowitz RJ, Rajagopal K, Whalen EJ. New roles for beta- arrestins in cell signaling: Not just seven-transmembrane receptors. Mol Cell 2006;24:643–52.
   PubMed Web of Science ®Google Scholar
• Luttrell LM. Composition and function of G protein-coupled receptor signalsomes controlling mitogen-activated protein kinase activity. J Mol Neurosci 2005;26:253–63.
   PubMed Web of Science ®Google Scholar
• Terrillon S, Bouvier M. Receptor activity-independent recruitment of β-arrestin reveals specific signaling modes. EMBO J 2004;23:3950–61.
   PubMed Web of Science ®Google Scholar
• Black JW, Leff P. Operational models of pharmacological agonist. Proc R Soc Lond [Biol] 1983;220:141–62.
   PubMed Web of Science ®Google Scholar
• Gesty-Palmer D, Chen M, Reiter E, Ahn S, Nelson CD, Wang S, Eckhardt AE, Cowan CL, Spurney RF, Luttrell LM, Lefkowitz RJ. Distinct β-arrestin- and G protein-dependent pathways for parathyroid hormone receptor-stimulated ERK1/2 activation. J Biol Chem 2006;281:10856–64.
   PubMed Web of Science ®Google Scholar
• Mackinnon AC, Waters C, Jodrell D, Haslett C, Sethi T. Bombesin and substance P analogues differentially regulate G-protein coupling to the bombesin receptor. J Biol Chem 2001;276:28083–91.
   PubMed Web of Science ®Google Scholar
• Tidgewell K, Groer CE, Harding WW, Lozama A, Schmidt M, Marquam A, Hiemstra J, Partilla JS, et al. Herkinorin analogues with differential b-arrestin-2 interactions. J Med Chem 2008;51:2421–31.
   Google Scholar
• Kenakin TP, Onaran O. The ligand paradox between affinity and efficacy: Can you be there and not make a difference? Trends Pharmacol Sci 2002;23:275–80.
   PubMed Web of Science ®Google Scholar