메뉴 건너뛰기




Volumn 9, Issue 2, 1997, Pages 134-142

How receptors talk to trimeric G proteins

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE DIPHOSPHATE; MEMBRANE RECEPTOR; SERPENTINE;

EID: 0030987069     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(97)80054-3     Document Type: Article
Times cited : (532)

References (66)
  • 3
    • 0029664589 scopus 로고    scopus 로고
    • The 2.0 Ȧ crystal structure of a heterotrimeric G protein
    • Lambright DG, Sondek J, Bohm A, Skiba NP, Hamm HE, Sigler PB: The 2.0 Ȧ crystal structure of a heterotrimeric G protein. Nature 1996, 379:311-319. These papers [2••,3••] present very similar 3D structures of two different Gα-βγ trimers, revealing the structure of Gβγ and defining the Gα-βγ binding interface. In addition, the structures define a probable membrane-oriented face of the trimer by identifying the likely locations of lipid modifications of Gα and Gγ, as well as the carboxyl terminus of Gα.
    • (1996) Nature , vol.379 , pp. 311-319
    • Lambright, D.G.1    Sondek, J.2    Bohm, A.3    Skiba, N.P.4    Hamm, H.E.5    Sigler, P.B.6
  • 4
    • 0029664921 scopus 로고    scopus 로고
    • Evolutionarily conserved Gαβγ binding surfaces support a model of the G protein-receptor complex
    • Lichtarge O, Bourne HR, Cohen FE: Evolutionarily conserved Gαβγ binding surfaces support a model of the G protein-receptor complex. Proc Natl Acad Sci USA 1996, 93:7507-7511. Patterns of conserved residues on the surface of Gα point to sites of two surfaces for interaction with other proteins. One of these surfaces interacts with βγ, as shown in the Gαβγ trimer structures. The other, presumably, interacts with serpentine receptors.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7507-7511
    • Lichtarge, O.1    Bourne, H.R.2    Cohen, F.E.3
  • 5
    • 0027318238 scopus 로고
    • Structural elements of Gα subunits that interact with Gβγ, receptors, and effectors
    • Conklin BR, Bourne HR: Structural elements of Gα subunits that interact with Gβγ, receptors, and effectors. Cell 1993, 73:631-641.
    • (1993) Cell , vol.73 , pp. 631-641
    • Conklin, B.R.1    Bourne, H.R.2
  • 6
    • 0029113832 scopus 로고
    • Transducin-α C-terminal mutations prevent activation by rhodopsin: A new assay using recombinant proteins expressed in cultured cells
    • Garcia PD, Onrust R, Bell SM, Sakmar TP, Bourne HR: Transducin-α C-terminal mutations prevent activation by rhodopsin: a new assay using recombinant proteins expressed in cultured cells. EMBO J 1995, 14:4460-4469.
    • (1995) EMBO J , vol.14 , pp. 4460-4469
    • Garcia, P.D.1    Onrust, R.2    Bell, S.M.3    Sakmar, T.P.4    Bourne, H.R.5
  • 10
    • 0029556994 scopus 로고
    • Projection structure of frog rhodopsin in two crystal forms
    • Schertler GF, Hargrave PA: Projection structure of frog rhodopsin in two crystal forms. Proc Natl Acad Sci USA 1995, 92:11578-11582. At somewhat higher resolution, this structure confirms the seven-helix bundle model inferred from the projection structure of cow rhodopsin [9]. Together, these structures powerfully constrain possible models of mechanisms of receptor activation by ligands and of G-protein activation by receptors.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11578-11582
    • Schertler, G.F.1    Hargrave, P.A.2
  • 11
    • 0027506471 scopus 로고
    • The probable arrangement of the helices in G protein-coupled receptors
    • Baldwin JM: The probable arrangement of the helices in G protein-coupled receptors. EMBO J 1993, 12:1693-1703.
    • (1993) EMBO J , vol.12 , pp. 1693-1703
    • Baldwin, J.M.1
  • 13
    • 0030606345 scopus 로고    scopus 로고
    • Structure determination of the fourth cytoplasmic loop and carboxyl terminal domain of bovine rhodopsin
    • Yeagle PL, Alderfer JL, Albert AD: Structure determination of the fourth cytoplasmic loop and carboxyl terminal domain of bovine rhodopsin. Mol Vision 1996, 2:12. On World Wide Web URL: http://www.emory.edu/molvis/v2/yeagle.
    • (1996) Mol Vision , vol.2 , pp. 12
    • Yeagle, P.L.1    Alderfer, J.L.2    Albert, A.D.3
  • 14
    • 0028230817 scopus 로고
    • Expanding horizons for receptors coupled to G proteins: Diversity and disease
    • Coughlin SR: Expanding horizons for receptors coupled to G proteins: diversity and disease. Curr Opin Cell Biol 1994, 6:191-197.
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 191-197
    • Coughlin, S.R.1
  • 15
    • 0028840683 scopus 로고
    • Functional coupling of a mammalian somatostatin receptor to the yeast pheromone response pathway
    • Price LA, Kajkowski EM, Hadcock JR, Ozenberger BA, Pausch MH: Functional coupling of a mammalian somatostatin receptor to the yeast pheromone response pathway. Mol Cell Biol 1995, 15:6188-6195.
    • (1995) Mol Cell Biol , vol.15 , pp. 6188-6195
    • Price, L.A.1    Kajkowski, E.M.2    Hadcock, J.R.3    Ozenberger, B.A.4    Pausch, M.H.5
  • 16
    • 0028920298 scopus 로고
    • Mapping the binding-site crevice of the dopamine D2 receptor by the substituted-cysteine accessibility method
    • Javitch JA, Fu D, Chen J, Karlin A: Mapping the binding-site crevice of the dopamine D2 receptor by the substituted-cysteine accessibility method. Neuron 1995, 14:825-831. See annotation [17•].
    • (1995) Neuron , vol.14 , pp. 825-831
    • Javitch, J.A.1    Fu, D.2    Chen, J.3    Karlin, A.4
  • 17
    • 0029757635 scopus 로고    scopus 로고
    • Residues in the seventh membrane-spanning segment of the dopamine D2 receptor accessible in the binding-site crevice
    • 2R) the potential crevice is bordered by at least three helices (TMs 3, 5, and 7) and extends all the way from extracellular fluid to cytoplasm.
    • (1996) Biochemistry , vol.35 , pp. 11278-11285
    • Fu, D.1    Ballesteros, J.A.2    Weinstein, H.3    Chen, J.4    Javitch, J.A.5
  • 19
    • 0028300554 scopus 로고
    • Active site-directed inactivation of constitutively active mutants of rhodopsin
    • Govardhan CP, Oprian DD: Active site-directed inactivation of constitutively active mutants of rhodopsin. J Biol Chem 1994, 269:6524-6527.
    • (1994) J Biol Chem , vol.269 , pp. 6524-6527
    • Govardhan, C.P.1    Oprian, D.D.2
  • 20
    • 0029085550 scopus 로고
    • Photoactivated state of rhodopsin and how it can form
    • Fahmy K, Siebert F, Sakmar TP: Photoactivated state of rhodopsin and how it can form. Biophys Chem 1995, 56:171-181.
    • (1995) Biophys Chem , vol.56 , pp. 171-181
    • Fahmy, K.1    Siebert, F.2    Sakmar, T.P.3
  • 21
    • 0027716597 scopus 로고
    • Photoactivated conformational changes in rhodopsin: A time-resolved spin label study
    • Farahbakhsh ZT, Hideg K,Hubbell WL: Photoactivated conformational changes in rhodopsin: a time-resolved spin label study. Science 1993, 262:1416-1419.
    • (1993) Science , vol.262 , pp. 1416-1419
    • Farahbakhsh, Z.T.1    Hideg, K.2    Hubbell, W.L.3
  • 22
    • 0029035661 scopus 로고
    • Mapping light-dependent structural changes in the cytoplasmic loop connecting helices C and D in rhodopsin: A site-directed spin labeling study
    • Farahbakhsh ZT, Ridge KD, Khorana HG, Hubbell WL: Mapping light-dependent structural changes in the cytoplasmic loop connecting helices C and D in rhodopsin: a site-directed spin labeling study. Biochemistry 1995, 34:8812-8819. See annotation [24••].
    • (1995) Biochemistry , vol.34 , pp. 8812-8819
    • Farahbakhsh, Z.T.1    Ridge, K.D.2    Khorana, H.G.3    Hubbell, W.L.4
  • 23
    • 0029818551 scopus 로고    scopus 로고
    • Structural features and light-dependent changes in the cytoplasmic interhelical E-F loop region of rhodopsin: A site-directed spin labeling study
    • Altenbach C, Yang K, Farrens DL, Khorana HG, Hubbell WL: Structural features and light-dependent changes in the cytoplasmic interhelical E-F loop region of rhodopsin: a site-directed spin labeling study. Biochemistry 1996, 35:12470-12478. See annotation [24••].
    • (1996) Biochemistry , vol.35 , pp. 12470-12478
    • Altenbach, C.1    Yang, K.2    Farrens, D.L.3    Khorana, H.G.4    Hubbell, W.L.5
  • 24
    • 0029907599 scopus 로고    scopus 로고
    • A light-activated conformational switch in rhodopsin
    • Farrens DL, Altenbach C, Yang K, Hubbell WL, Khorana HG: A light-activated conformational switch in rhodopsin. Science 1996, 274:768-770. These (and other) papers [22•,23•,24••] from a collaboration between the Khorana and Hubbell laboratories present evidence that the activation of rhodopsin causes TMs 3 and 6 to move, as rigid bodies, relative to the rest of the seven-helix bundle; in addition, activation is associated with movement of these two TMs away from one another.
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 25
    • 0028108981 scopus 로고
    • Investigation of structure and dynamics in membrane proteins using site-directed spin labeling
    • Hubbell WL, Altenbach C: Investigation of structure and dynamics in membrane proteins using site-directed spin labeling. Curr Opin Struct Biol 1994, 4:566-573.
    • (1994) Curr Opin Struct Biol , vol.4 , pp. 566-573
    • Hubbell, W.L.1    Altenbach, C.2
  • 26
    • 0029756165 scopus 로고    scopus 로고
    • Specific tryptophan UV-absorbance changes are probes of the transition of rhodopsin to its active state
    • Lin SW, Sakmar TP: Specific tryptophan UV-absorbance changes are probes of the transition of rhodopsin to its active state. Biochemistry 1996, 35:11149-11159.
    • (1996) Biochemistry , vol.35 , pp. 11149-11159
    • Lin, S.W.1    Sakmar, T.P.2
  • 27
    • 0029778268 scopus 로고    scopus 로고
    • Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F
    • Sheikh SP, Zvyaga TA, Lichtarge O, Sakmar TP, Bourne HR: Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F. Nature 1996, 383:347-350.
    • (1996) Nature , vol.383 , pp. 347-350
    • Sheikh, S.P.1    Zvyaga, T.A.2    Lichtarge, O.3    Sakmar, T.P.4    Bourne, H.R.5
  • 28
    • 0028946950 scopus 로고
    • Characterization of rhodopsin mutants that bind transducin but fail to induce GTP nucleotide uptake. Classification of mutant pigments by fluorescence, nucleotide release, and flash-induced light-scattering assays
    • Ernst OP, Hofmann KP, Sakmar TP: Characterization of rhodopsin mutants that bind transducin but fail to induce GTP nucleotide uptake. Classification of mutant pigments by fluorescence, nucleotide release, and flash-induced light-scattering assays. J Biol Chem 1995, 270:10580-10586. Using a variety of biophysical and biochemical techniques, the authors of this paper show that receptor-promoted release of GDP from the G-protein trimer requires more than just association of the trimer with a serpentine receptor. Although the mechanism by which the receptor induces GDP release is unknown, it probably requires the ERY (single-letter code for amino acids) sequence located at the junction of ic2 and TM3.
    • (1995) J Biol Chem , vol.270 , pp. 10580-10586
    • Ernst, O.P.1    Hofmann, K.P.2    Sakmar, T.P.3
  • 30
    • 0028061193 scopus 로고
    • A conserved carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin
    • Amis S, Fahmy K, Hofmann KP, Sakmar TP: A conserved carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin. J Biol Chem 1994, 269:23879-23881.
    • (1994) J Biol Chem , vol.269 , pp. 23879-23881
    • Amis, S.1    Fahmy, K.2    Hofmann, K.P.3    Sakmar, T.P.4
  • 31
    • 0026780339 scopus 로고
    • Structure and function in rhodopsin. Studies of the interaction between the rhodopsin cytoplasmic domain and transducin
    • Franke RR, Sakmar TP, Graham RM, Khorana HG: Structure and function in rhodopsin. Studies of the interaction between the rhodopsin cytoplasmic domain and transducin. J Biol Chem 1992, 267:14767-14774.
    • (1992) J Biol Chem , vol.267 , pp. 14767-14774
    • Franke, R.R.1    Sakmar, T.P.2    Graham, R.M.3    Khorana, H.G.4
  • 32
    • 0027270898 scopus 로고
    • Regulation of the rhodopsin-transducin interaction by a highly conserved carboxylic acid group
    • Fahmy K, Sakmar TP: Regulation of the rhodopsin-transducin interaction by a highly conserved carboxylic acid group. Biochemistry 1993, 32:7229-7236.
    • (1993) Biochemistry , vol.32 , pp. 7229-7236
    • Fahmy, K.1    Sakmar, T.P.2
  • 33
    • 0026592357 scopus 로고
    • 1B-adrenergic receptor by all amino acid substitutions at a single site. Evidence for a region which constrains receptor activation
    • 1B-adrenergic receptor by all amino acid substitutions at a single site. Evidence for a region which constrains receptor activation. J Biol Chem 1992, 267:1430-1433.
    • (1992) J Biol Chem , vol.267 , pp. 1430-1433
    • Kjelsberg, M.A.1    Cotecchia, S.2    Ostrowski, J.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 35
    • 12044260162 scopus 로고
    • Mutations that alter the third cytoplasmic loop of the α-factor receptor lead to a constitutive and hypersensitive phenotype
    • Boone C, Davis NG, Sprague GF Jr: Mutations that alter the third cytoplasmic loop of the α-factor receptor lead to a constitutive and hypersensitive phenotype. Proc Natl Acad Sci USA 1993, 90:9921-9925.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9921-9925
    • Boone, C.1    Davis, N.G.2    Sprague G.F., Jr.3
  • 36
    • 0029832901 scopus 로고    scopus 로고
    • Transmembrane regions V and VI of the human luteinizing hormone receptor are required for constitutive activation by a mutation in the third intracellular loop
    • Kudo M, Osuga Y, Kobilka BK, Hsueh AJW: Transmembrane regions V and VI of the human luteinizing hormone receptor are required for constitutive activation by a mutation in the third intracellular loop. J Biol Chem 1996, 271:22470-22478.
    • (1996) J Biol Chem , vol.271 , pp. 22470-22478
    • Kudo, M.1    Osuga, Y.2    Kobilka, B.K.3    Hsueh, A.J.W.4
  • 37
    • 0026752495 scopus 로고
    • Different β-subunits determine G-protein interaction with transmembrane receptors
    • Kleuss C, Scherübl H, Hescheler J, Schultz G, Wittig B: Different β-subunits determine G-protein interaction with transmembrane receptors. Nature 1992, 358:424-426.
    • (1992) Nature , vol.358 , pp. 424-426
    • Kleuss, C.1    Scherübl, H.2    Hescheler, J.3    Schultz, G.4    Wittig, B.5
  • 38
    • 0027530916 scopus 로고
    • Selectivity in signal transduction determined by y subunits of heterotrimeric G proteins
    • Kleuss C, Scherübl H, Hescheler J, Schultz G, Wittig B: Selectivity in signal transduction determined by y subunits of heterotrimeric G proteins. Science 1993, 259:832-834.
    • (1993) Science , vol.259 , pp. 832-834
    • Kleuss, C.1    Scherübl, H.2    Hescheler, J.3    Schultz, G.4    Wittig, B.5
  • 39
    • 0023716027 scopus 로고
    • Site of G protein binding to rhodopsin mapped with synthetic peptides from the a subunit
    • Hamm HE, Deretic D, Arendt A, Hargrave PA, Koenig B, Hofmann KP: Site of G protein binding to rhodopsin mapped with synthetic peptides from the a subunit Science 1988, 241:832-835.
    • (1988) Science , vol.241 , pp. 832-835
    • Hamm, H.E.1    Deretic, D.2    Arendt, A.3    Hargrave, P.A.4    Koenig, B.5    Hofmann, K.P.6
  • 45
    • 0028361809 scopus 로고
    • Chimeric muscarinic cholinergic:beta-adrenergic receptors that are functionally promiscuous among G proteins
    • Wong SK, Ross EM: Chimeric muscarinic cholinergic:beta-adrenergic receptors that are functionally promiscuous among G proteins. J Biol Chem 1994, 269:18968-18976.
    • (1994) J Biol Chem , vol.269 , pp. 18968-18976
    • Wong, S.K.1    Ross, E.M.2
  • 46
    • 0029784196 scopus 로고    scopus 로고
    • The luteinizing hormone/ chorionic gonadotropin receptor has distinct transmembrane conductors for cAMP and inositol phosphate signals
    • Gilchrrst RL, Ryu K, Ji I, Ji TH: The luteinizing hormone/ chorionic gonadotropin receptor has distinct transmembrane conductors for cAMP and inositol phosphate signals. J Biol Chem 1996, 271:19283-19287.
    • (1996) J Biol Chem , vol.271 , pp. 19283-19287
    • Gilchrrst, R.L.1    Ryu, K.2    Ji, I.3    Ji, T.H.4
  • 47
    • 0030049488 scopus 로고    scopus 로고
    • Constitutive activation of a single effector pathway: Evidence for multiple activation states of a G protein-coupled receptor
    • Perez DM, Hwa J, Gaivin R, Mathur M, Brown F, Graham RM: Constitutive activation of a single effector pathway: evidence for multiple activation states of a G protein-coupled receptor. Mol Pharmacol 1996, 49:112-122.
    • (1996) Mol Pharmacol , vol.49 , pp. 112-122
    • Perez, D.M.1    Hwa, J.2    Gaivin, R.3    Mathur, M.4    Brown, F.5    Graham, R.M.6
  • 48
    • 0030614427 scopus 로고    scopus 로고
    • Receptor and βγ binding sites in the a subunit of the retinal G protein transducin
    • t that probably participate in the protein-protein interactions required for activation by rhodopsin. One of these surfaces interacts with Gβγ in G-protein trimers. The other presumably interacts with the receptor.
    • (1997) Science , vol.275 , pp. 381-384
    • Onrust, R.1    Herzmark, P.2    Chi, P.3    Garcia, P.D.4    Lichtarge, O.5    Kingsley, C.6    Bourne, H.R.7
  • 49
    • 0029589916 scopus 로고
    • Identification of a receptor/G-protein contact site critical for signaling specificity and G-protein activation
    • Liu J, Conklin BR, Blin N, Yun J, Wess J: Identification of a receptor/G-protein contact site critical for signaling specificity and G-protein activation. Prac Natl Acad Sci USA 1995, 92:11642-11646. Experiments with interfering peptides and site-directed mutations identify regions of receptor and G-protein subunits that are important for receptor-G-protein coupling. To understand receptor-mediated activation of G proteins, however, we must identify specific residues of the two proteins that interact directly with one another. As noted in Table 3, this paper identifies one such contact by showing functional complementation between an amino acid sequence substituted in the carboxy-terminal tail of a Gα and a separate sequence substituted at the junction of ic3 and TM6 in a receptor.
    • (1995) Prac Natl Acad Sci USA , vol.92 , pp. 11642-11646
    • Liu, J.1    Conklin, B.R.2    Blin, N.3    Yun, J.4    Wess, J.5
  • 50
    • 0029096818 scopus 로고
    • Mutational analysis of the relative orientation of transmembrane helices I and VII in G protein-coupled receptors
    • Liu J, Schoneberg T, Van Rhee M, Wess J: Mutational analysis of the relative orientation of transmembrane helices I and VII in G protein-coupled receptors. J Biol Chem 1995, 270:19532-19539.
    • (1995) J Biol Chem , vol.270 , pp. 19532-19539
    • Liu, J.1    Schoneberg, T.2    Van Rhee, M.3    Wess, J.4
  • 52
    • 0028822684 scopus 로고
    • A general method for mapping tertiary contacts between amino acid residues in membrane-embedded proteins
    • Yu H, Kono M, McKee TD, Oprian DD: A general method for mapping tertiary contacts between amino acid residues in membrane-embedded proteins. Biochemistry 1995, 34:14963-14969.
    • (1995) Biochemistry , vol.34 , pp. 14963-14969
    • Yu, H.1    Kono, M.2    McKee, T.D.3    Oprian, D.D.4
  • 53
    • 0029680797 scopus 로고    scopus 로고
    • Structure and function in rhodopsin. Cysteines 65 and 316 are in proximity in a rhodopsin mutant as indicated by disulfide formation and interactions between attached spin labels
    • Yang K, Farrens DL, Altenbach C, Farahbakhsh ZT, Hubbell WL, Khorana HG: Structure and function in rhodopsin. Cysteines 65 and 316 are in proximity in a rhodopsin mutant as indicated by disulfide formation and interactions between attached spin labels. Biochemistry 1996, 35:14040-14046.
    • (1996) Biochemistry , vol.35 , pp. 14040-14046
    • Yang, K.1    Farrens, D.L.2    Altenbach, C.3    Farahbakhsh, Z.T.4    Hubbell, W.L.5    Khorana, H.G.6
  • 54
    • 0028800729 scopus 로고
    • Conversion of antagonist-binding site to metal-ion site in the tachykinin NK-1 receptor
    • Elling CE, Nielsen SM, Schwartz TW: Conversion of antagonist-binding site to metal-ion site in the tachykinin NK-1 receptor. Nature 1995, 374:74-77.
    • (1995) Nature , vol.374 , pp. 74-77
    • Elling, C.E.1    Nielsen, S.M.2    Schwartz, T.W.3
  • 55
    • 0029957956 scopus 로고    scopus 로고
    • Connectivity and orientation of the seven helical bundle in the tachykinin NK-1 receptor probed by zinc site engineering
    • Elling CE, Schwartz TW: Connectivity and orientation of the seven helical bundle in the tachykinin NK-1 receptor probed by zinc site engineering. EMBO J 1996, 15:6213-6219.
    • (1996) EMBO J , vol.15 , pp. 6213-6219
    • Elling, C.E.1    Schwartz, T.W.2
  • 56
    • 0030028517 scopus 로고    scopus 로고
    • Arrangement of transmembrane domains in adrenergic receptors. Similarity to bacteriorhodopsin
    • Mizobe T, Maze M, Lam V, Suryanarayana S, Kobilka BK: Arrangement of transmembrane domains in adrenergic receptors. Similarity to bacteriorhodopsin. J Biol Chem 1996, 271:2387-2389.
    • (1996) J Biol Chem , vol.271 , pp. 2387-2389
    • Mizobe, T.1    Maze, M.2    Lam, V.3    Suryanarayana, S.4    Kobilka, B.K.5
  • 57
    • 0027964847 scopus 로고
    • Insertion mutagenesis as a tool to predict the secondary structure of a muscarinic receptor domain determining specificity of G-protein coupling
    • Bluml K, Mutschler E, Wess J: Insertion mutagenesis as a tool to predict the secondary structure of a muscarinic receptor domain determining specificity of G-protein coupling. Proc Natl Acad Sci USA 1994, 91:7980-7984.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7980-7984
    • Bluml, K.1    Mutschler, E.2    Wess, J.3
  • 58
    • 0030039837 scopus 로고    scopus 로고
    • Structure of a G-protein-coupling domain of a muscarinic receptor predicted by random saturation mutagenesis
    • Hill-Eubanks D, Burstein ES, Spalding TA, Brauner-Osborne H, Brann MR: Structure of a G-protein-coupling domain of a muscarinic receptor predicted by random saturation mutagenesis. J Biol Chem 1996, 271:3058-3065.
    • (1996) J Biol Chem , vol.271 , pp. 3058-3065
    • Hill-Eubanks, D.1    Burstein, E.S.2    Spalding, T.A.3    Brauner-Osborne, H.4    Brann, M.R.5
  • 59
    • 0029818639 scopus 로고    scopus 로고
    • Structure and function in rhodopsin. Single cysteine substitution mutants in the cytoplasmic interhelical E-F loop region show position-specific effects in transducin activation
    • Yang K, Farrens D, Hubbell WL, Khorana HG: Structure and function in rhodopsin. Single cysteine substitution mutants in the cytoplasmic interhelical E-F loop region show position-specific effects in transducin activation. Biochemistry 1996, 35:12464-12469.
    • (1996) Biochemistry , vol.35 , pp. 12464-12469
    • Yang, K.1    Farrens, D.2    Hubbell, W.L.3    Khorana, H.G.4
  • 60
    • 0028812838 scopus 로고
    • Structure of the third cytoplasmic loop of bovine rhodopsin
    • Yeagle PL, Alderfer JL, Albert AD: Structure of the third cytoplasmic loop of bovine rhodopsin. Biochemistry 1995, 34:14621-14625.
    • (1995) Biochemistry , vol.34 , pp. 14621-14625
    • Yeagle, P.L.1    Alderfer, J.L.2    Albert, A.D.3
  • 61
    • 0029848323 scopus 로고    scopus 로고
    • Peptide mimetic of the third cytoplasmic loop of the PTH/PTHrP receptor
    • Mierke DF, Royo M, Pellegrini M, Sun H, Corev M: Peptide mimetic of the third cytoplasmic loop of the PTH/PTHrP receptor. J Am Chem Soc 1996, 118:8998-9004.
    • (1996) J Am Chem Soc , vol.118 , pp. 8998-9004
    • Mierke, D.F.1    Royo, M.2    Pellegrini, M.3    Sun, H.4    Corev, M.5
  • 62
    • 0028814543 scopus 로고
    • Structure-function of muscarinic receptor coupling to G proteins. Random saturation mutagenesis identifies a critical determinant of receptor affinity for G proteins
    • Burstein ES, Spalding TA, Hill-Eubanks D, Brann MR: Structure-function of muscarinic receptor coupling to G proteins. Random saturation mutagenesis identifies a critical determinant of receptor affinity for G proteins. J Biol Chem 1995, 270:3141-3146.
    • (1995) J Biol Chem , vol.270 , pp. 3141-3146
    • Burstein, E.S.1    Spalding, T.A.2    Hill-Eubanks, D.3    Brann, M.R.4
  • 63
    • 0028172426 scopus 로고
    • Binding of an alpha 2 adrenergic receptor third intracellular loop peptide to G beta and the amino terminus of G alpha
    • Taylor JM, Jacob-Mosier GG, Lawton RG, Remmers AE, Neubig RR: Binding of an alpha 2 adrenergic receptor third intracellular loop peptide to G beta and the amino terminus of G alpha. J Biol Chem 1994, 269:27618-27624.
    • (1994) J Biol Chem , vol.269 , pp. 27618-27624
    • Taylor, J.M.1    Jacob-Mosier, G.G.2    Lawton, R.G.3    Remmers, A.E.4    Neubig, R.R.5
  • 64
    • 0030064529 scopus 로고    scopus 로고
    • Receptor and membrane interaction sites on Gβ. A receptor-derived peptide binds to the carboxyl terminus
    • Taylor JM, Jacob-Mosier GG, Lawton RG, Van Dort M, Neubig RR: Receptor and membrane interaction sites on Gβ. A receptor-derived peptide binds to the carboxyl terminus. J Biol Chem 1996, 271:3336-3339.
    • (1996) J Biol Chem , vol.271 , pp. 3336-3339
    • Taylor, J.M.1    Jacob-Mosier, G.G.2    Lawton, R.G.3    Van Dort, M.4    Neubig, R.R.5
  • 65
    • 0026786080 scopus 로고
    • Rhodopsin/transducin interactions. I. Characterization of the binding of the transducin-beta gamma subunit complex to rhodopsin using fluorescence spectroscopy
    • Phillips WJ, Cerione RA: Rhodopsin/transducin interactions. I. Characterization of the binding of the transducin-beta gamma subunit complex to rhodopsin using fluorescence spectroscopy. J Biol Chem 1992, 267:17032-17039.
    • (1992) J Biol Chem , vol.267 , pp. 17032-17039
    • Phillips, W.J.1    Cerione, R.A.2
  • 66
    • 0028296886 scopus 로고
    • A C-terminal peptide of bovine rhodopsin binds to the transducin alpha-subunit and facilitates its activation
    • Phillips WJ, Cerione RA: A C-terminal peptide of bovine rhodopsin binds to the transducin alpha-subunit and facilitates its activation. Biochem J 1994, 299:351-357.
    • (1994) Biochem J , vol.299 , pp. 351-357
    • Phillips, W.J.1    Cerione, R.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.