Chapter 11 G Protein-Coupled Receptors: Structure and Function of Signal-Transducing Proteins

作者: Eric M. Parker , Elliott M. Ross

DOI: 10.1016/S0070-2161(08)60173-2

关键词: G proteinBiologyClass C GPCRReceptorRhodopsin-like receptors5-HT2 receptorChemokine receptorBiochemistryG protein-coupled receptorG protein-coupled receptor kinase

摘要: Publisher Summary This chapter reviews the knowledge of structure G protein-coupled receptors and structural features that are responsible for various functions ascribed to cell-surface receptors, particularly it emphasizes on β-adrenergic receptor, because it, along with rhodopsin, is most extensively studied receptors. Cell-surface utilize proteins represent a large diverse group proteins. They include many neurotransmitter (e.g, adrenergic, muscarinic cholinergic, serotonergic, peptidergic receptors); pituitary protein hormones, eicosanoids, rhodopsins; pheromone in yeast slime molds. All these integral membrane glycoproteins display significant functional homology. The application molecular cloning techniques study has led elucidation primary several striking aspect presence seven stretches hydrophobic amino acids. In case rhodopsins, biophysical, proteolytic, immunocytochemical, chemical modification experiments have shown regions largely helical span lipid bilayer.

参考文章(49)
J B C Findlay, D J C Pappin, The opsin family of proteins. Biochemical Journal. ,vol. 238, pp. 625- 642 ,(1986) , 10.1042/BJ2380625
R. A. Dixon, I. S. Sigal, M. R. Candelore, R. B. Register, W. Scattergood, E. Rands, C. D. Strader, Structural features required for ligand binding to the beta-adrenergic receptor. The EMBO Journal. ,vol. 6, pp. 3269- 3275 ,(1987) , 10.1002/J.1460-2075.1987.TB02645.X
R A Cerione, C Staniszewski, J L Benovic, R J Lefkowitz, M G Caron, P Gierschik, R Somers, A M Spiegel, J Codina, L Birnbaumer, Specificity of the functional interactions of the beta-adrenergic receptor and rhodopsin with guanine nucleotide regulatory proteins reconstituted in phospholipid vesicles. Journal of Biological Chemistry. ,vol. 260, pp. 1493- 1500 ,(1985) , 10.1016/S0021-9258(18)89619-3
CD Strader, RA Dixon, AH Cheung, MR Candelore, AD Blake, IS Sigal, Mutations that uncouple the beta-adrenergic receptor from Gs and increase agonist affinity. Journal of Biological Chemistry. ,vol. 262, pp. 16439- 16443 ,(1987) , 10.1016/S0021-9258(18)49275-7
T Higashijima, S Uzu, T Nakajima, E M Ross, Mastoparan, a peptide toxin from wasp venom, mimics receptors by activating GTP-binding regulatory proteins (G proteins). Journal of Biological Chemistry. ,vol. 263, pp. 6491- 6494 ,(1988) , 10.1016/S0021-9258(18)68669-7
B F O'Dowd, M Hnatowich, J W Regan, W M Leader, M G Caron, R J Lefkowitz, Site-directed mutagenesis of the cytoplasmic domains of the human beta 2-adrenergic receptor. Localization of regions involved in G protein-receptor coupling. Journal of Biological Chemistry. ,vol. 263, pp. 15985- 15992 ,(1988) , 10.1016/S0021-9258(18)37546-X
P C Sternweis, J D Robishaw, Isolation of two proteins with high affinity for guanine nucleotides from membranes of bovine brain Journal of Biological Chemistry. ,vol. 259, pp. 13806- 13813 ,(1984) , 10.1016/S0021-9258(18)89817-9
RC Rubenstein, SK Wong, EM Ross, The hydrophobic tryptic core of the beta-adrenergic receptor retains Gs regulatory activity in response to agonists and thiols. Journal of Biological Chemistry. ,vol. 262, pp. 16655- 16662 ,(1987) , 10.1016/S0021-9258(18)49305-2