Abstract
G-protein-coupled receptors (GPCRs) are a diverse family of integral membrane proteins that are believed to share many structural and functional properties. Upon stimulation, these receptors can transmit a signal across the bilayer that results in the activation of enzymes or transport systems via a G-protein. The size of the family is increasing rapidly and includes the neurotransmitter receptors (e.g., adrenergic, muscarinic acetylcholine, neurokinins, dopamine, serotonin) as well as the visual and odorant receptors (e.g., rhodopsin).
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Altenbach C, Marti T, Khorana HG, Hubbell WL (1990) Structural studies on transmembrane proteins 2. Spin labeling of bacteriorhodopsin mutants at unique cysteines. Science 248:1088–1092.
Brett M, Findlay JBC (1979) Investigation of the organisation of rhodopsin in sheep photoreceptor membranes using cross-linking agents. Biochem J 117:215–223.
Brett M, Findlay JBC (1983) isolation and characterization of the CNBr peptides from the proteolytically derived N terminal fragment of ovine rhodopsin. Biochem J 211:661–670.
Cornette JL, Cease KB, Margalit H, Spouge JL, Berzofsky JA, DeLisi C (1987) Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins. J Mol Biol 195:659–685.
Davison MD, Findlay JBC (1986a) Modification of ovine opsin with the photosensitive hydrophobic probe l-azido-4[125I]iodobenzene. Biochem J 234:413–420.
Davison MD, Findlay JBC (1986b) Identification of the sites in opsin modified photoactivated l-azido-4[125I]iodobenzene. Biochem J 236:389–395.
Donnelly D, Johnson MJ, Blundell TL, Saunders J (1989) An analysis of the periodicity of conserved residues in sequence alignments of G-protein coupled receptors. FEBS Lett 251:109–116.
Donnelly D, Overington JP, Ruffle SV, Nugent JHA, Blundell TL (1993) Modelling α-helical transmembrane domains — the calculation and use of substitution tables for lipid facing residues. Protein Sci 2:55–70.
Eisenberg D, Weiss RM, Terwilliger TC (1984) The hydrophobic moment detects periodicity in protein hydrophobicity. Proc Natl Acad Sci USA 81:140–144.
Findlay JBC, Brett M, Pappin DJC (1981) Primary structure of C-terminal functional sites in ovine rhodopsin. Nature 293:314–316.
Findlay JBC, Pappin DJC (1986) The opsin family of proteins. Biochem J 238: 625–642.
Findlay J, Eliopoulos E (1990) Three-dimensional modelling of G protein-linked receptors. TIPS 11:492–499.
Gamier J, Osguthorpe DJ, Robson B (1978) Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J Mol Biol 120:97–120.
Grötzinger J, Engelss M, Jacoby E, Wollmer A, Straßburger W (1991) A model for the C5a receptor and for its interaction with the ligand. Protein Sci 4:767–771.
Henderson R, Unwin PTN (1975) Three-dimensional model of purple membrane obtained by electron microscopy. Nature 257:28–32.
Henderson R, Baldwin JM, Ceska TA, Zemlin F, Beckmann E, Downing KH (1990) Model for the structure of bacteriorhodopsin based on high resolution electron cyro-microscopy. J Mol Biol 213:899–929.
Hibert MF, Trumpp-Kallmeyer S, Bruinvels A, Hoflack J (1991) Three-dimensional models of neurotransmitter G-binding protein-coupled receptors. Molecular Pharmacology 40:8–15.
Karnik SS, Khorana HG (1990) Cysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin. J Biol Chem 265:17520–17524.
Komiya H, Yeates TO, Rees DC, Allen JP, Feher G (1988) Structure of the reaction centre from Rhodobacter sphaeroides R-26 and 2.4.1: symmetry relations and sequence comparisons between different species. Proc Natl Acad Sci USA 85:9012–9016.
MaloneyHuss K, Lybrand TP (1992) Three-dimensional structure for the β2 adrenergic receptor protein based on computer modeling studies. J Mol Biol 225:859–871.
Ovchinnikov YuA, Abdulaev NG, Bogachuk AS (1988) Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitylated. FEBS Lett 230:1–5.
Pappin DJC, Eliopoulos E, Brett M, Findlay JBC (1984) A structural model for ovine rhodopsin. Int J Biol Macromol 6:73–76.
Rees DC, DeAntonio L, Eisenberg D (1989) Hydrophobic organization of membrane proteins. Science 245:510–513.
Strader CD, Candelore MR, Hill WS, Sigal IS, Dixon RAF (1989) Identification of two serine residues involved in agonist activation of the β-adrrenergic receptor. J Biol Chem 264:13572–13578.
Strader CD, Gaffney T, Sugg EE, Candlemore MR, Keys R, Patchett AA, Dixon RAF (1991) Allele specific activation of genetically engineered receptors. J Biol Chem 266:5–8.
Stubbs GW, Smith HG, Litman BJ (1976) Alkyl glucosides as effective solubilizing agents for bovine rhodopsin — a comparison of several commonly used detergents. Biochim Biophys Acta 246:46–56.
Sutcliffe MJ, Haneef I, Carney D, Blundeli TL (1987a) Knowledge-based modelling of homologous proteins 1. Three-dimensional frameworks derived from the simultaneous superposition of multiple structures. Prot Engng 1:377–384.
Sutcliffe MJ, Hayes FRF, Blundell TL (1987b) Knowledge-based modelling of homologous proteins 2. Rules for the conformation of substituted sidechains. Prot Engng 1:385–392.
Tadayyon M, Zhang Y, Gnaneshan S, Hunt L, Mehraein-Ghomi F, Broome-Smith JK (1992) β-Lactamase fusion analysis of membrane protein assembly. Biochem Soc Trans 20:598–601.
Wang JK, McDowell JHM, Hargrave PA (1980) Site of attachment of 11-cis-retinal in bovine rhodopsin. Biochem 19:5111–5117.
Wang H-y, Lipfert L, Malbon CC, Bahouth S (1989) Sire-directed anti-peptide antibodies define the topography of the β-adrenergic receptor. J Biol Chem 264:14424–14431.
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Findlay, J.B.C., Donnelly, D. (1993). The Superfamily: Molecular Modelling. In: Dickey, B.F., Birnbaumer, L. (eds) GTPases in Biology II. Handbook of Experimental Pharmacology, vol 108 / 2. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-78345-6_2
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DOI: https://doi.org/10.1007/978-3-642-78345-6_2
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