메뉴 건너뛰기




Volumn 70, Issue 3, 2006, Pages 838-850

Mutagenesis within helix 6 of the human β1-adrenergic receptor identifies lysine324 as a residue involved in imparting the high-affinity binding state of agonists

Author keywords

[No Author keywords available]

Indexed keywords

ADENYLATE CYCLASE; ADRENALIN; ALANINE; ARGININE; ASPARTIC ACID; BETA 1 ADRENERGIC RECEPTOR; BETA 1 ADRENERGIC RECEPTOR STIMULATING AGENT; DOBUTAMINE; G PROTEIN COUPLED RECEPTOR; GLUTAMIC ACID; ISOETARINE; ISOPRENALINE; LYSINE; MUTANT PROTEIN; NORADRENALIN; PARTIAL AGONIST; TERBUTALINE; TYROSINE;

EID: 33747597571     PISSN: 0026895X     EISSN: 15210111     Source Type: Journal    
DOI: 10.1124/mol.106.025346     Document Type: Article
Times cited : (5)

References (40)
  • 1
    • 0001198946 scopus 로고
    • Drug-receptor interaction and relation between stimulus and effect
    • Ariens EJ ed Academic Press, New York
    • Ariens EJ, Simonis AM, and van Rossum JM (1964) Drug-receptor interaction and relation between stimulus and effect, in Molecular Pharmacology, vol 1 (Ariens EJ ed) pp 394-466, Academic Press, New York.
    • (1964) Molecular Pharmacology , vol.1 , pp. 394-466
    • Ariens, E.J.1    Simonis, A.M.2    Van Rossum, J.M.3
  • 2
    • 0031565726 scopus 로고    scopus 로고
    • An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors
    • Baldwin JM, Schertler GF, and Unger VM (1997) An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors. J Mol Biol 272:144-164.
    • (1997) J Mol Biol , vol.272 , pp. 144-164
    • Baldwin, J.M.1    Schertler, G.F.2    Unger, V.M.3
  • 4
    • 0030987069 scopus 로고    scopus 로고
    • How receptors talk to trimeric G proteins
    • Bourne HR (1997) How receptors talk to trimeric G proteins. Curr Opin Cell Biol 9:134-142.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 134-142
    • Bourne, H.R.1
  • 5
    • 0002060353 scopus 로고
    • The relation between classical and cooperative models for drug action
    • Rang HP ed University Park, Baltimore
    • Colquhoun D (1973) The relation between classical and cooperative models for drug action, in Drug Receptors (Rang HP ed) pp 149-182, University Park, Baltimore.
    • (1973) Drug Receptors , pp. 149-182
    • Colquhoun, D.1
  • 6
    • 0019137579 scopus 로고
    • A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled β-adrenergic receptor
    • De Lean A, Stadel JM, and Lefkowitz RJ (1980) A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled β-adrenergic receptor. J Biol Chem 255:7108-7117.
    • (1980) J Biol Chem , vol.255 , pp. 7108-7117
    • De Lean, A.1    Stadel, J.M.2    Lefkowitz, R.J.3
  • 8
    • 0030634725 scopus 로고    scopus 로고
    • Engineering of metal-ion sites as distance constraints in structural and functional analysis of 7TM receptors
    • Elling CE, Thirstrup K, Nielsen SM, Hjorth SA, and Shwartz TW (1997) Engineering of metal-ion sites as distance constraints in structural and functional analysis of 7TM receptors. Fold Res 2:S76-S80.
    • (1997) Fold Res , vol.2
    • Elling, C.E.1    Thirstrup, K.2    Nielsen, S.M.3    Hjorth, S.A.4    Shwartz, T.W.5
  • 9
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens DL, Altenbach C, Yang K, Hubbell WL, and Khorana HG (1996) Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science (Wash DC) 274:768-770.
    • (1996) Science (Wash DC) , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 11
    • 0023841905 scopus 로고    scopus 로고
    • A single amino acid substitution in rhodopsin (lysine 248 to leucine) prevents activation of transducin
    • Franke RR, Sakmar TP, Oparain DD, and Khorana HG (1998) A single amino acid substitution in rhodopsin (lysine 248 to leucine) prevents activation of transducin. J Biol Chem 263:2119-2122.
    • (1998) J Biol Chem , vol.263 , pp. 2119-2122
    • Franke, R.R.1    Sakmar, T.P.2    Oparain, D.D.3    Khorana, H.G.4
  • 12
    • 0017874045 scopus 로고
    • Pharmacological characterization of receptors: Its relation to radioligand-binding studies
    • Furchgott RF (1978) Pharmacological characterization of receptors: its relation to radioligand-binding studies. Fed Proc 37:115-120.
    • (1978) Fed Proc , vol.37 , pp. 115-120
    • Furchgott, R.F.1
  • 14
  • 15
    • 0032541084 scopus 로고    scopus 로고
    • G protein-coupled receptors II. Mechanism of agonist activation
    • Gether U and Kobilka BK (1998) G protein-coupled receptors II. Mechanism of agonist activation. J Biol Chem 273:17979-17982.
    • (1998) J Biol Chem , vol.273 , pp. 17979-17982
    • Gether, U.1    Kobilka, B.K.2
  • 17
    • 0031956092 scopus 로고    scopus 로고
    • Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy
    • Gordon GW, Berry G, Liang XH, Levin B, and Herman B (1998) Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy. Biophys J 74:2702-2713.
    • (1998) Biophys J , vol.74 , pp. 2702-2713
    • Gordon, G.W.1    Berry, G.2    Liang, X.H.3    Levin, B.4    Herman, B.5
  • 18
    • 4344567339 scopus 로고    scopus 로고
    • Quantitative fluorescence resonance energy transfer (FRET) measurement with acceptor photobleaching and spectral unmixing
    • Gu Y, Di WL, Kelsell DP, and Zicha D (2004) Quantitative fluorescence resonance energy transfer (FRET) measurement with acceptor photobleaching and spectral unmixing. J Microsc 215:162-173.
    • (2004) J Microsc , vol.215 , pp. 162-173
    • Gu, Y.1    Di, W.L.2    Kelsell, D.P.3    Zicha, D.4
  • 19
    • 0008534153 scopus 로고
    • Adenylate cyclase permanently uncoupled from hormone receptors in a novel variant of S49 mouse lymphoma cells
    • Haga T, Ross EM, Anderson HJ, and Gilman AG (1977) Adenylate cyclase permanently uncoupled from hormone receptors in a novel variant of S49 mouse lymphoma cells. Proc Natl Acad Sci USA 74:2016-2020.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 2016-2020
    • Haga, T.1    Ross, E.M.2    Anderson, H.J.3    Gilman, A.G.4
  • 22
    • 3142773613 scopus 로고    scopus 로고
    • Rhodopsin activation exposes a key hydrophobic binding site for the transducin α-subunit terminus
    • Janz JM and Farrens DL (2004) Rhodopsin activation exposes a key hydrophobic binding site for the transducin α-subunit terminus. J Biol Chem 279:29767-29773.
    • (2004) J Biol Chem , vol.279 , pp. 29767-29773
    • Janz, J.M.1    Farrens, D.L.2
  • 23
    • 0028920298 scopus 로고
    • 2 receptor by the substituted-cysteine accessibility method
    • 2 receptor by the substituted-cysteine accessibility method. Neuron 14:825-831.
    • (1995) Neuron , vol.14 , pp. 825-831
    • Javitch, J.A.1    Fu, D.2    Chen, J.3    Karlin, A.4
  • 24
    • 0018862848 scopus 로고
    • A quantitative analysis of beta-adrenergic receptor interactions: Resolution of high and low affinity states of the receptor by computer modeling of ligand binding data
    • Kent RS, De Lean A, and Lefkowitz RJ (1980) A quantitative analysis of beta-adrenergic receptor interactions: resolution of high and low affinity states of the receptor by computer modeling of ligand binding data. Mol Pharmacol 17:14-23.
    • (1980) Mol Pharmacol , vol.17 , pp. 14-23
    • Kent, R.S.1    De Lean, A.2    Lefkowitz, R.J.3
  • 25
    • 0034846540 scopus 로고    scopus 로고
    • Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy
    • Kenworthy AK (2001) Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy. Methods 24:289-296.
    • (2001) Methods , vol.24 , pp. 289-296
    • Kenworthy, A.K.1
  • 27
    • 0026754015 scopus 로고
    • Accurate modeling of protein conformation by automatic segment matching
    • Levitt M (1992) Accurate modeling of protein conformation by automatic segment matching. J Mol Biol 226:507-533.
    • (1992) J Mol Biol , vol.226 , pp. 507-533
    • Levitt, M.1
  • 28
    • 0030815133 scopus 로고    scopus 로고
    • Raster 3D: Photorealistic molecular graphics
    • Merrit EA and Bacon DJ (1997) Raster 3D: photorealistic molecular graphics. Methods Enzymol 227:505-524.
    • (1997) Methods Enzymol , vol.227 , pp. 505-524
    • Merrit, E.A.1    Bacon, D.J.2
  • 30
    • 0025193724 scopus 로고
    • Identification of a Gs-protein coupling domain to the β-adrenergic receptor using site-specific synthetic peptides
    • Palm D, Munch G, Malek D, Dees C, and Hekman M (1990) Identification of a Gs-protein coupling domain to the β-adrenergic receptor using site-specific synthetic peptides. FEBS Lett 261:294-298.
    • (1990) FEBS Lett , vol.261 , pp. 294-298
    • Palm, D.1    Munch, G.2    Malek, D.3    Dees, C.4    Hekman, M.5
  • 37
  • 38
    • 0021327070 scopus 로고
    • Beta-adrenergic receptors: Biochemical mechanisms of physiological regulation
    • Stiles GL, Caron MG, and Lefkowitz RJ (1984) Beta-adrenergic receptors: biochemical mechanisms of physiological regulation. Physiol Rev 64:661-743.
    • (1984) Physiol Rev , vol.64 , pp. 661-743
    • Stiles, G.L.1    Caron, M.G.2    Lefkowitz, R.J.3
  • 39
    • 0015535998 scopus 로고
    • On the analysis of pharmacological experiments in terms of an allosteric receptor model
    • Thron CD (1973) On the analysis of pharmacological experiments in terms of an allosteric receptor model. Mol Pharmacol 9:1-9.
    • (1973) Mol Pharmacol , vol.9 , pp. 1-9
    • Thron, C.D.1
  • 40
    • 0028128646 scopus 로고
    • Characterization of rhodopsin-transducin interaction: A mutant rhodopsin photoproduct with a protonated Schiff base activates transducin
    • Zuyga TA, Fahmy K, and Sakmar TP (1994) Characterization of rhodopsin-transducin interaction: a mutant rhodopsin photoproduct with a protonated Schiff base activates transducin. Biochemistry 33:9753-9761.
    • (1994) Biochemistry , vol.33 , pp. 9753-9761
    • Zuyga, T.A.1    Fahmy, K.2    Sakmar, T.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.