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Volumn 288, Issue 45, 2013, Pages 32449-32465

Molecular basis of cannabinoid CB1 receptor coupling to the G protein heterotrimer Gαiβγ; Identification of key CB1 contacts with the C-terminal helix α5 of Gαi

Author keywords

[No Author keywords available]

Indexed keywords

ADRENERGIC RECEPTORS; CONFORMATIONAL CHANGE; COUPLING ACTIVITIES; G PROTEIN ACTIVATION; G PROTEIN COUPLED RECEPTORS; INTRACELLULAR LOOP; MOLECULAR DYNAMICS SIMULATIONS; STRUCTURAL MODELING;

EID: 84887443683     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.489153     Document Type: Article
Times cited : (25)

References (97)
  • 1
    • 0038024615 scopus 로고    scopus 로고
    • The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints
    • Fredriksson, R., Lagerström, M. C., Lundin, L. G., and Schiöth, H. B. (2003) The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. Mol. Pharmacol. 63, 1256-1272
    • (2003) Mol. Pharmacol , vol.63 , pp. 1256-1272
    • Fredriksson, R.1    Lagerström, M.C.2    Lundin, L.G.3    Schiöth, H.B.4
  • 2
    • 80052158550 scopus 로고    scopus 로고
    • Independent HHsearch, Needleman-Wunschbased, and motif analyses reveal the overall hierarchy for most of the G protein-coupled receptor families
    • Nordström, K. J., Sällman Almén, M., Edstam, M. M., Fredriksson, R., and Schiöth, H. B. (2011) Independent HHsearch, Needleman-Wunschbased, and motif analyses reveal the overall hierarchy for most of the G protein-coupled receptor families. Mol. Biol. Evol. 28, 2471-2480
    • (2011) Mol. Biol. Evol , vol.28 , pp. 2471-2480
    • Nordström, K.J.1    Sällman Almén, M.2    Edstam, M.M.3    Fredriksson, R.4    Schiöth, H.B.5
  • 4
    • 0027132717 scopus 로고
    • The 2.2 Å crystal structure of transducin-α complexed with GTPγS
    • Noel, J. P., Hamm, H. E., and Sigler, P. B. (1993) The 2.2 Å crystal structure of transducin-α complexed with GTPγS. Nature 366, 654-663
    • (1993) Nature , vol.366 , pp. 654-663
    • Noel, J.P.1    Hamm, H.E.2    Sigler, P.B.3
  • 6
    • 37549016836 scopus 로고    scopus 로고
    • Heterotrimeric G protein activation by G-protein-coupled receptors
    • Oldham, W. M., and Hamm, H. E. (2008) Heterotrimeric G protein activation by G-protein-coupled receptors. Nat. Rev. Mol. Cell Biol. 9, 60-71
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , pp. 60-71
    • Oldham, W.M.1    Hamm, H.E.2
  • 7
    • 17644402459 scopus 로고    scopus 로고
    • Transduction of receptor signals by β-arrestins
    • Lefkowitz, R. J., and Shenoy, S. K. (2005) Transduction of receptor signals by β-arrestins. Science 308, 512-517
    • (2005) Science , vol.308 , pp. 512-517
    • Lefkowitz, R.J.1    Shenoy, S.K.2
  • 8
    • 84855901533 scopus 로고    scopus 로고
    • Molecular mechanism of β-arrestin-biased agonism at seven-transmembrane receptors
    • Reiter, E., Ahn, S., Shukla, A. K., and Lefkowitz, R. J. (2012) Molecular mechanism of β-arrestin-biased agonism at seven-transmembrane receptors. Annu. Rev. Pharmacol. Toxicol. 52, 179-197
    • (2012) Annu. Rev. Pharmacol. Toxicol , vol.52 , pp. 179-197
    • Reiter, E.1    Ahn, S.2    Shukla, A.K.3    Lefkowitz, R.J.4
  • 9
    • 71749083052 scopus 로고    scopus 로고
    • Rhodopsin and the others. A historical perspective on structural studies of G protein-coupled receptors
    • Costanzi, S., Siegel J, Tikhonova, I. G., and Jacobson, K. A. (2009) Rhodopsin and the others. A historical perspective on structural studies of G protein-coupled receptors. Curr. Pharm. Des. 15, 3994-4002
    • (2009) Curr. Pharm. des , vol.15 , pp. 3994-4002
    • Costanzi, S.1    Siegel, J.2    Tikhonova, I.G.3    Jacobson, K.A.4
  • 10
    • 58149203324 scopus 로고    scopus 로고
    • Discovery of new GPCR biology. One receptor structure at a time
    • Hanson, M. A., and Stevens, R. C. (2009) Discovery of new GPCR biology. One receptor structure at a time. Structure 17, 8-14
    • (2009) Structure , vol.17 , pp. 8-14
    • Hanson, M.A.1    Stevens, R.C.2
  • 14
    • 0027318238 scopus 로고
    • Structural elements of Gα subunits that interact with Gβγ, receptors, and effectors
    • Conklin, B. R., and Bourne, H. R. (1993) Structural elements of Gα subunits that interact with Gβγ, receptors, and effectors. Cell 73, 631-641
    • (1993) Cell , vol.73 , pp. 631-641
    • Conklin, B.R.1    Bourne, H.R.2
  • 15
    • 77955583625 scopus 로고    scopus 로고
    • Electron paramagnetic resonance studies of functionally active, nitroxide spin-labeled peptide analogues of the C-terminus of a G-protein α subunit
    • Van Eps, N., Anderson, L. L., Kisselev, O. G., Baranski, T. J., Hubbell, W. L., and Marshall, G. R. (2010) Electron paramagnetic resonance studies of functionally active, nitroxide spin-labeled peptide analogues of the C-terminus of a G-protein α subunit. Biochemistry 49, 6877-6886
    • (2010) Biochemistry , vol.49 , pp. 6877-6886
    • Van Eps, N.1    Anderson, L.L.2    Kisselev, O.G.3    Baranski, T.J.4    Hubbell, W.L.5    Marshall, G.R.6
  • 16
    • 0023164972 scopus 로고
    • Effects of Mg2+ and the βγ-subunit complex on the interactions of guanine nucleotides with G proteins
    • Higashijima, T., Ferguson, K. M., Sternweis, P. C., Smigel, M. D., and Gilman, A. G. (1987) Effects of Mg2+ and the βγ-subunit complex on the interactions of guanine nucleotides with G proteins. J. Biol. Chem. 262, 762-766
    • (1987) J. Biol. Chem , vol.262 , pp. 762-766
    • Higashijima, T.1    Ferguson, K.M.2    Sternweis, P.C.3    Smigel, M.D.4    Gilman, A.G.5
  • 17
    • 0025878961 scopus 로고
    • Molecular cloning of a human cannabinoid receptor which is also expressed in testis
    • Gérard, C. M., Mollereau, C., Vassart, G., and Parmentier, M. (1991) Molecular cloning of a human cannabinoid receptor which is also expressed in testis. Biochem. J. 279, 129-134
    • (1991) Biochem. J , vol.279 , pp. 129-134
    • Gérard, C.M.1    Mollereau, C.2    Vassart, G.3    Parmentier, M.4
  • 19
    • 79952567365 scopus 로고    scopus 로고
    • The cannabinoid type-1 receptor carboxyl-terminus, more than just a tail
    • Stadel, R., Ahn, K. H., and Kendall, D. A. (2011) The cannabinoid type-1 receptor carboxyl-terminus, more than just a tail. J. Neurochem. 117, 1-18
    • (2011) J. Neurochem , vol.117 , pp. 1-18
    • Stadel, R.1    Ahn, K.H.2    Kendall, D.A.3
  • 20
    • 0034333417 scopus 로고    scopus 로고
    • Inverse agonist properties of N-(piperidin-1-yl)-5-(4-chlorophenyl)- 1-(2,4-dichlorophenyl)-4-methyl-1H-pyrazole-3-carboxamide HCl (SR141716A) and 1-(2-chlorophenyl)-4-cyano-5-(4-methoxyphenyl)- 1H-pyrazole-3-carboxylic acid phenylamide (CP-272871) for the CB(1) cannabinoid receptor
    • Meschler, J. P., Kraichely, D. M., Wilken, G. H., and Howlett, A. C. (2000) Inverse agonist properties of N-(piperidin-1-yl)-5-(4-chlorophenyl)- 1-(2,4-dichlorophenyl)-4-methyl-1H-pyrazole-3-carboxamide HCl (SR141716A) and 1-(2-chlorophenyl)-4-cyano-5-(4-methoxyphenyl)- 1H-pyrazole-3-carboxylic acid phenylamide (CP-272871) for the CB(1) cannabinoid receptor. Biochem. Pharmacol. 60, 1315-1323
    • (2000) Biochem. Pharmacol , vol.60 , pp. 1315-1323
    • Meschler, J.P.1    Kraichely, D.M.2    Wilken, G.H.3    Howlett, A.C.4
  • 21
    • 77950644306 scopus 로고    scopus 로고
    • CB(1) cannabinoid receptors and their associated proteins
    • Howlett, A. C., Blume, L. C., and Dalton, G. D. (2010) CB(1) cannabinoid receptors and their associated proteins. Curr. Med. Chem. 17, 1382-1393
    • (2010) Curr. Med. Chem , vol.17 , pp. 1382-1393
    • Howlett, A.C.1    Blume, L.C.2    Dalton, G.D.3
  • 22
    • 0032756226 scopus 로고    scopus 로고
    • Agonist selective regulation of G proteins by cannabinoid CB(1) and CB(2) receptors
    • Glass, M., and Northup, J. K. (1999) Agonist selective regulation of G proteins by cannabinoid CB(1) and CB(2) receptors. Mol. Pharmacol. 56, 1362-1369
    • (1999) Mol. Pharmacol , vol.56 , pp. 1362-1369
    • Glass, M.1    Northup, J.K.2
  • 23
    • 0023797851 scopus 로고
    • Structural and functional relationships of guanosine triphosphate binding proteins
    • Pfeuffer, T., and Helmreich, E. J. (1988) Structural and functional relationships of guanosine triphosphate binding proteins. Curr. Top. Cell Regul. 29, 129-216
    • (1988) Curr. Top. Cell Regul , vol.29 , pp. 129-216
    • Pfeuffer, T.1    Helmreich, E.J.2
  • 24
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen, C., and Okayama, H. (1987) High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell Biol. 7, 2745-2752
    • (1987) Mol. Cell Biol , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 25
    • 33646363596 scopus 로고    scopus 로고
    • Mutations of CB1 T210 produce active and inactive receptor forms. Correlations with ligand affinity, receptor stability, and cellular localization
    • D'Antona, A. M., Ahn, K. H., and Kendall, D. A. (2006) Mutations of CB1 T210 produce active and inactive receptor forms. Correlations with ligand affinity, receptor stability, and cellular localization. Biochemistry 45, 5606-5617
    • (2006) Biochemistry , vol.45 , pp. 5606-5617
    • D'Antona, A.M.1    Ahn, K.H.2    Kendall, D.A.3
  • 26
    • 84859479825 scopus 로고    scopus 로고
    • Allosteric modulator ORG27569 induces CB1 cannabinoid receptor high affinity agonist binding state, receptor internalization, and Gi protein-independent ERK1/2 kinase activation
    • Ahn, K. H., Mahmoud, M. M., and Kendall, D. A. (2012) Allosteric modulator ORG27569 induces CB1 cannabinoid receptor high affinity agonist binding state, receptor internalization, and Gi protein-independent ERK1/2 kinase activation. J. Biol. Chem. 287, 12070-12082
    • (2012) J. Biol. Chem , vol.287 , pp. 12070-12082
    • Ahn, K.H.1    Mahmoud, M.M.2    Kendall, D.A.3
  • 27
    • 84872546888 scopus 로고    scopus 로고
    • Functional residues essential for the activation of the CB1 cannabinoid receptor
    • Shim, J.-Y., and Padgett, L. (2013) Functional residues essential for the activation of the CB1 cannabinoid receptor. Methods Enzymol. 520, 337-355
    • (2013) Methods Enzymol , vol.520 , pp. 337-355
    • Shim, J.-Y.1    Padgett, L.2
  • 28
    • 77950517052 scopus 로고    scopus 로고
    • Aconserved protonation-induced switch can trigger "ionic-lock" formation in adrenergic receptors
    • Vanni, S., Neri, M., Tavernelli, I., and Rothlisberger, U. (2010)Aconserved protonation-induced switch can trigger "ionic-lock" formation in adrenergic receptors. J. Mol. Biol. 397, 1339-1349
    • (2010) J. Mol. Biol , vol.397 , pp. 1339-1349
    • Vanni, S.1    Neri, M.2    Tavernelli, I.3    Rothlisberger, U.4
  • 29
    • 0033061256 scopus 로고    scopus 로고
    • Mutation of a highly conserved aspartic acid in the β2 adrenergic receptor. Constitutive activation, structural instability, and conformational rearrangement of transmembrane segment 6
    • Rasmussen, S. G., Jensen, A. D., Liapakis, G., Ghanouni, P., Javitch, J. A., and Gether, U. (1999) Mutation of a highly conserved aspartic acid in the β2 adrenergic receptor. Constitutive activation, structural instability, and conformational rearrangement of transmembrane segment 6. Mol. Pharmacol. 56, 175-184
    • (1999) Mol. Pharmacol , vol.56 , pp. 175-184
    • Rasmussen, S.G.1    Jensen, A.D.2    Liapakis, G.3    Ghanouni, P.4    Javitch, J.A.5    Gether, U.6
  • 31
    • 80053038272 scopus 로고    scopus 로고
    • Identification of essential cannabinoid-binding domains. Structural insights into early dynamic events in receptor activation
    • Shim, J.-Y., Bertalovitz, A. C., and Kendall, D. A. (2011) Identification of essential cannabinoid-binding domains. Structural insights into early dynamic events in receptor activation. J. Biol. Chem. 286, 33422-33435
    • (2011) J. Biol. Chem , vol.286 , pp. 33422-33435
    • Shim, J.-Y.1    Bertalovitz, A.C.2    Kendall, D.A.3
  • 34
    • 79959564813 scopus 로고    scopus 로고
    • Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation
    • Lebon, G., Warne, T., Edwards, P. C., Bennett, K., Langmead, C. J., Leslie, A. G., and Tate, C. G. (2011) Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation. Nature 474, 521-525
    • (2011) Nature , vol.474 , pp. 521-525
    • Lebon, G.1    Warne, T.2    Edwards, P.C.3    Bennett, K.4    Langmead, C.J.5    Leslie, A.G.6    Tate, C.G.7
  • 35
    • 0035935802 scopus 로고    scopus 로고
    • Calculating free energies using average force
    • Darve, E., and Pohorille, A. (2001) Calculating free energies using average force. J. Chem. Phys. 115, 9169-9183
    • (2001) J. Chem. Phys , vol.115 , pp. 9169-9183
    • Darve, E.1    Pohorille, A.2
  • 37
    • 0037167584 scopus 로고    scopus 로고
    • Structure of the third intracellular loop of the human cannabinoid 1 receptor
    • Ulfers, A. L., McMurry, J. L., Kendall, D. A., and Mierke, D. F. (2002) Structure of the third intracellular loop of the human cannabinoid 1 receptor. Biochemistry 41, 11344-11350
    • (2002) Biochemistry , vol.41 , pp. 11344-11350
    • Ulfers, A.L.1    McMurry, J.L.2    Kendall, D.A.3    Mierke, D.F.4
  • 40
    • 0037799206 scopus 로고    scopus 로고
    • Keeping G proteins at bay. A complex between G proteincoupled receptor kinase 2 and Gβγ
    • Lodowski, D. T., Pitcher, J. A., Capel, W. D., Lefkowitz, R. J., and Tesmer, J. J. (2003) Keeping G proteins at bay. A complex between G proteincoupled receptor kinase 2 and Gβγ. Science 300, 1256-1262
    • (2003) Science , vol.300 , pp. 1256-1262
    • Lodowski, D.T.1    Pitcher, J.A.2    Capel, W.D.3    Lefkowitz, R.J.4    Tesmer, J.J.5
  • 41
    • 0029878720 scopus 로고    scopus 로고
    • VMD. Visual molecular dynamics
    • 27-28
    • Humphrey, W., Dalke, A., and Schulten, K. (1996) VMD. Visual molecular dynamics. J. Mol. Graph. 14, 33-38, 27-28
    • (1996) J. Mol. Graph , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 42
    • 67649412152 scopus 로고    scopus 로고
    • Transmembrane helical domain of the cannabinoid CB1 receptor
    • Shim, J.-Y. (2009) Transmembrane helical domain of the cannabinoid CB1 receptor. Biophys. J. 96, 3251-3262
    • (2009) Biophys. J , vol.96 , pp. 3251-3262
    • Shim, J.-Y.1
  • 43
    • 3242881211 scopus 로고    scopus 로고
    • SuperPose.Asimple server for sophisticated structural superposition
    • Maiti, R., Van Domselaar, G. H., Zhang, H., and Wishart, D. S. (2004) SuperPose.Asimple server for sophisticated structural superposition. Nucleic Acids Res. 32, W590-W594
    • (2004) Nucleic Acids Res , vol.32
    • Maiti, R.1    Van Domselaar, G.H.2    Zhang, H.3    Wishart, D.S.4
  • 45
    • 39849104464 scopus 로고    scopus 로고
    • Effect of NaCl and KCl on phosphatidylcholine and phosphatidylethanolamine lipid membranes. Insight from atomic-scale simulations for understanding salt-induced effects in the plasma membrane
    • Gurtovenko, A. A., Vattulainen, I. (2008) Effect of NaCl and KCl on phosphatidylcholine and phosphatidylethanolamine lipid membranes. Insight from atomic-scale simulations for understanding salt-induced effects in the plasma membrane. J. Phys. Chem. B 112, 1953-1962
    • (2008) J. Phys. Chem. B , vol.112 , pp. 1953-1962
    • Gurtovenko, A.A.1    Vattulainen, I.2
  • 46
    • 33646446451 scopus 로고    scopus 로고
    • Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains
    • Kucerka, N., Tristram-Nagle, S., and Nagle, J. F. (2005) Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains. J. Membr. Biol. 208, 193-202
    • (2005) J. Membr. Biol , vol.208 , pp. 193-202
    • Kucerka, N.1    Tristram-Nagle, S.2    Nagle, J.F.3
  • 47
    • 0030876951 scopus 로고    scopus 로고
    • Phosphatidylcholine acyl unsaturation modulates the decrease in interfacial elasticity induced by cholesterol
    • Smaby, J. M., Momsen, M. M., Brockman, H. L., and Brown, R. E. (1997) Phosphatidylcholine acyl unsaturation modulates the decrease in interfacial elasticity induced by cholesterol. Biophys. J. 73, 1492-1505
    • (1997) Biophys. J , vol.73 , pp. 1492-1505
    • Smaby, J.M.1    Momsen, M.M.2    Brockman, H.L.3    Brown, R.E.4
  • 48
    • 0002001503 scopus 로고    scopus 로고
    • The liquid crystallographic structure of fluid lipid bilayer membranes
    • (Merz, K. M., and Roux, B., eds), Birkhäuser, Boston
    • White, S. H., and Wiener, M. C. (1996) The liquid crystallographic structure of fluid lipid bilayer membranes. in Membrane Structure and Dynamics (Merz, K. M., and Roux, B., eds) pp. 127-144, Birkhäuser, Boston
    • (1996) Membrane Structure and Dynamics , pp. 127-144
    • White, S.H.1    Wiener, M.C.2
  • 49
    • 80052903046 scopus 로고    scopus 로고
    • Accelerating protein docking in ZDOCK using an advanced 3D convolution library
    • Pierce, B. G., Hourai, Y., and Weng, Z. (2011) Accelerating protein docking in ZDOCK using an advanced 3D convolution library. PLoS One 6, e24657
    • (2011) PLoS One , vol.6
    • Pierce, B.G.1    Hourai, Y.2    Weng, Z.3
  • 50
    • 33751119043 scopus 로고    scopus 로고
    • The receptor-bound "empty pocket" state of the heterotrimeric G-protein α-subunit is conformationally dynamic
    • Abdulaev, N. G., Ngo, T., Ramon, E., Brabazon, D. M., Marino, J. P., and Ridge, K. D. (2006) The receptor-bound "empty pocket" state of the heterotrimeric G-protein α-subunit is conformationally dynamic. Biochemistry 45, 12986-12997
    • (2006) Biochemistry , vol.45 , pp. 12986-12997
    • Abdulaev, N.G.1    Ngo, T.2    Ramon, E.3    Brabazon, D.M.4    Marino, J.P.5    Ridge, K.D.6
  • 53
    • 0034250744 scopus 로고    scopus 로고
    • An improved empirical potential energy function for molecular simulations of phospholipids
    • Feller, S., and MacKerell, A. D., Jr. (2000) An improved empirical potential energy function for molecular simulations of phospholipids. J. Phys. Chem. B 104, 7510-7515
    • (2000) J. Phys. Chem. B , vol.104 , pp. 7510-7515
    • Feller, S.1    MacKerell Jr., A.D.2
  • 54
    • 1642576012 scopus 로고    scopus 로고
    • Improved treatment of the protein backbone in empirical force fields
    • MacKerell, A. D., Jr., Feig, M., and Brooks, C. L., 3rd (2004) Improved treatment of the protein backbone in empirical force fields. J. Am. Chem. Soc. 126, 698-699
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 698-699
    • MacKerell Jr., A.D.1    Feig, M.2    Brooks III, C.L.3
  • 55
    • 84865723813 scopus 로고    scopus 로고
    • Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone φ, ψ and sidechain χ(1) and χ(2) dihedral angles
    • Best, R. B., Zhu, X., Shim, J., Lopes, P. E., Mittal, J., Feig, M., and Mackerell, A. D. Jr. (2012) Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone φ, ψ and sidechain χ(1) and χ(2) dihedral angles. J. Chem. Theory Comput. 8, 3257-3273
    • (2012) J. Chem. Theory Comput , vol.8 , pp. 3257-3273
    • Best, R.B.1    Zhu, X.2    Shim, J.3    Lopes, P.E.4    Mittal, J.5    Feig, M.6    Mackerell Jr., A.D.7
  • 58
    • 0036930078 scopus 로고    scopus 로고
    • Molecular dynamics investigation of primary photoinduced events in the activation of rhodopsin
    • Saam, J., Tajkhorshid, E., Hayashi, S., and Schulten K. (2002) Molecular dynamics investigation of primary photoinduced events in the activation of rhodopsin. Biophys. J. 83, 3097-3112
    • (2002) Biophys. J , vol.83 , pp. 3097-3112
    • Saam, J.1    Tajkhorshid, E.2    Hayashi, S.3    Schulten, K.4
  • 59
    • 36449007836 scopus 로고
    • Protocol for classical molecular dynamics simulations of nano-junctions in solution
    • Feller, S. E., Zhang, Y., Pastor, R. W., and Brooks, B. R. (1995) Protocol for classical molecular dynamics simulations of nano-junctions in solution. J. Chem. Phys. 103, 4613-4621
    • (1995) J. Chem. Phys , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.2    Pastor, R.W.3    Brooks, B.R.4
  • 60
    • 0001538909 scopus 로고
    • Canonical dynamics. Equilibrium phase-space distributions
    • Hoover, W. G. (1985) Canonical dynamics. Equilibrium phase-space distributions. Phys. Rev. A31, 1695-1697
    • (1985) Phys. Rev , vol.A31 , pp. 1695-1697
    • Hoover, W.G.1
  • 62
    • 33646650705 scopus 로고
    • Reversible multiple time scale molecular-dynamics
    • Tuckerman, M., Berne, B. J., and Martyna, G. J. (1992) Reversible multiple time scale molecular-dynamics. J. Chem. Phys. 97, 1990-2001
    • (1992) J. Chem. Phys , vol.97 , pp. 1990-2001
    • Tuckerman, M.1    Berne, B.J.2    Martyna, G.J.3
  • 64
    • 0031436245 scopus 로고    scopus 로고
    • Crystal structure of the adenylyl cyclase activator Gsα
    • Sunahara, R. K., Tesmer, J. J., Gilman, A. G., and Sprang, S. R. (1997) Crystal structure of the adenylyl cyclase activator Gsα. Science 278, 1943-1947
    • (1997) Science , vol.278 , pp. 1943-1947
    • Sunahara, R.K.1    Tesmer, J.J.2    Gilman, A.G.3    Sprang, S.R.4
  • 65
    • 0035800850 scopus 로고    scopus 로고
    • Activation of the β2-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6
    • Ballesteros, J. A., Jensen, A. D., Liapakis, G., Rasmussen, S. G., Shi, L., Gether, U., and Javitch, J. A. (2001) Activation of the β2-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6. J. Biol. Chem. 276, 29171-29177
    • (2001) J. Biol. Chem , vol.276 , pp. 29171-29177
    • Ballesteros, J.A.1    Jensen, A.D.2    Liapakis, G.3    Rasmussen, S.G.4    Shi, L.5    Gether, U.6    Javitch, J.A.7
  • 69
    • 47049084133 scopus 로고    scopus 로고
    • Internal hydration increases during activation of the G-proteincoupled receptor rhodopsin
    • Grossfield, A., Pitman, M. C., Feller, S. E., Soubias, O., and Gawrisch, K. (2008) Internal hydration increases during activation of the G-proteincoupled receptor rhodopsin. J. Mol. Biol. 381, 478-486
    • (2008) J. Mol. Biol , vol.381 , pp. 478-486
    • Grossfield, A.1    Pitman, M.C.2    Feller, S.E.3    Soubias, O.4    Gawrisch, K.5
  • 70
    • 84873032055 scopus 로고    scopus 로고
    • Molecular basis for dramatic changes in cannabinoid CB1 G protein- coupled receptor activation upon single and double point mutations
    • Scott, C. E., Abrol, R., Ahn, K. H., Kendall, D. A., and Goddard, W. A., 3rd (2013) Molecular basis for dramatic changes in cannabinoid CB1 G protein- coupled receptor activation upon single and double point mutations. Protein Sci. 22, 101-113
    • (2013) Protein Sci , vol.22 , pp. 101-113
    • Scott, C.E.1    Abrol, R.2    Ahn, K.H.3    Kendall, D.A.4    Goddard III, W.A.5
  • 71
    • 84869035098 scopus 로고    scopus 로고
    • Probing the interaction of SR141716A with the CB1 receptor
    • Shim, J.-Y., Bertalovitz, A. C., and Kendall, D. A. (2012) Probing the interaction of SR141716A with the CB1 receptor. J. Biol. Chem. 287, 38741-38754
    • (2012) J. Biol. Chem , vol.287 , pp. 38741-38754
    • Shim, J.-Y.1    Bertalovitz, A.C.2    Kendall, D.A.3
  • 72
    • 0031808129 scopus 로고    scopus 로고
    • Mutation of a highly conserved aspartate residue in the second transmembrane domain of the cannabinoid receptors, CB1 and CB2, disrupts G-protein coupling
    • Tao, Q., and Abood, M. E. (1998) Mutation of a highly conserved aspartate residue in the second transmembrane domain of the cannabinoid receptors, CB1 and CB2, disrupts G-protein coupling. J. Pharmacol. Exp. Ther. 285, 651-658
    • (1998) J. Pharmacol. Exp. Ther , vol.285 , pp. 651-658
    • Tao, Q.1    Abood, M.E.2
  • 73
    • 0032819441 scopus 로고    scopus 로고
    • Amutation in the second transmembrane region of the CB1 receptor selectively disrupts G protein signaling and prevents receptor internalization
    • Roche, J. P., Bounds, S., Brown, S., and Mackie, K. (1999)Amutation in the second transmembrane region of the CB1 receptor selectively disrupts G protein signaling and prevents receptor internalization. Mol. Pharmacol. 56, 611-618
    • (1999) Mol. Pharmacol , vol.56 , pp. 611-618
    • Roche, J.P.1    Bounds, S.2    Brown, S.3    Mackie, K.4
  • 74
    • 0037174606 scopus 로고    scopus 로고
    • β2 adrenergic receptor activation. Modulation of the proline kink in transmembrane 6 by a rotamer toggle switch
    • Shi, L., Liapakis, G., Xu, R., Guarnieri, F., Ballesteros, J. A., and Javitch, J. A. (2002) β2 adrenergic receptor activation. Modulation of the proline kink in transmembrane 6 by a rotamer toggle switch. J. Biol. Chem. 277, 40989-40996
    • (2002) J. Biol. Chem , vol.277 , pp. 40989-40996
    • Shi, L.1    Liapakis, G.2    Xu, R.3    Guarnieri, F.4    Ballesteros, J.A.5    Javitch, J.A.6
  • 75
    • 9144224914 scopus 로고    scopus 로고
    • Structural mimicry in class A G protein-coupled receptor rotamer toggle switches. The importance of the F3.36(201)/ W6.48(357) interaction in cannabinoid CB1 receptor activation
    • McAllister, S. D., Hurst, D. P., Barnett-Norris, J., Lynch, D., Reggio, P. H., and Abood, M. E. (2004) Structural mimicry in class A G protein-coupled receptor rotamer toggle switches. The importance of the F3.36(201)/ W6.48(357) interaction in cannabinoid CB1 receptor activation. J. Biol. Chem. 279, 48024-48037
    • (2004) J. Biol. Chem , vol.279 , pp. 48024-48037
    • McAllister, S.D.1    Hurst, D.P.2    Barnett-Norris, J.3    Lynch, D.4    Reggio, P.H.5    Abood, M.E.6
  • 76
    • 78751487961 scopus 로고    scopus 로고
    • A structural insight into the reorientation of transmembrane domains 3 and 5 during family A G proteincoupled receptor activation
    • Sansuk, K., Deupi, X., Torrecillas, I. R., Jongejan, A., Nijmeijer, S., Bakker, R. A., Pardo, L., and Leurs, R. (2011) A structural insight into the reorientation of transmembrane domains 3 and 5 during family A G proteincoupled receptor activation. Mol. Pharmacol. 79, 262-269
    • (2011) Mol. Pharmacol , vol.79 , pp. 262-269
    • Sansuk, K.1    Deupi, X.2    Torrecillas, I.R.3    Jongejan, A.4    Nijmeijer, S.5    Bakker, R.A.6    Pardo, L.7    Leurs, R.8
  • 78
    • 70349810683 scopus 로고    scopus 로고
    • Structural evidence for a sequential release mechanism for activation of heterotrimeric G proteins
    • Kapoor, N., Menon, S. T., Chauhan, R., Sachdev, P., and Sakmar, T. P. (2009) Structural evidence for a sequential release mechanism for activation of heterotrimeric G proteins. J. Mol. Biol. 393, 882-897
    • (2009) J. Mol. Biol , vol.393 , pp. 882-897
    • Kapoor, N.1    Menon, S.T.2    Chauhan, R.3    Sachdev, P.4    Sakmar, T.P.5
  • 80
    • 0027379660 scopus 로고
    • Hydrophobic amino acid in the i2 loop plays a key role in receptor-G protein coupling
    • Moro, O., Lameh, J., Högger, P., and Sadée, W. (1993) Hydrophobic amino acid in the i2 loop plays a key role in receptor-G protein coupling. J. Biol. Chem. 268, 22273-22276
    • (1993) J. Biol. Chem , vol.268 , pp. 22273-22276
    • Moro, O.1    Lameh, J.2    Högger, P.3    Sadée, W.4
  • 81
    • 78649417771 scopus 로고    scopus 로고
    • Structural determinants in the second intracellular loop of the human cannabinoid CB1 receptor mediate selective coupling to Gs and Gi
    • Chen, X. P., Yang, W., Fan, Y., Luo, J. S., Hong, K., Wang, Z., Yan, J. F., Chen, X., Lu, J. X., Benovic, J. L., and Zhou, N. M. (2010) Structural determinants in the second intracellular loop of the human cannabinoid CB1 receptor mediate selective coupling to Gs and Gi. Br. J. Pharmacol. 161, 1817-1834
    • (2010) Br. J. Pharmacol , vol.161 , pp. 1817-1834
    • Chen, X.P.1    Yang, W.2    Fan, Y.3    Luo, J.S.4    Hong, K.5    Wang, Z.6    Yan, J.F.7    Chen, X.8    Lu, J.X.9    Benovic, J.L.10    Zhou, N.M.11
  • 82
    • 0031565726 scopus 로고    scopus 로고
    • An α-carbon template for the transmembrane helices in the rhodopsin family of G-protein- coupled receptors
    • Baldwin, J. M., Schertler, G. F., and Unger, V. M. (1997) An α-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
  • 83
    • 0026630552 scopus 로고
    • Detection of G protein-activator regions in M4 subtype muscarinic, cholinergic, and α2-adrenergic receptors based upon characteristics in primary structure
    • Okamoto, T., and Nishimoto, I. (1992) Detection of G protein-activator regions in M4 subtype muscarinic, cholinergic, and α2-adrenergic receptors based upon characteristics in primary structure. J. Biol. Chem. 267, 8342-8346
    • (1992) J. Biol. Chem , vol.267 , pp. 8342-8346
    • Okamoto, T.1    Nishimoto, I.2
  • 84
    • 0033574084 scopus 로고    scopus 로고
    • Regulation ofGi by the CB1 cannabinoid receptor C-terminal juxtamembrane region. Structural requirements determined by peptide analysis
    • Mukhopadhyay, S., Cowsik, S. M., Lynn, A. M., Welsh, W. J., and Howlett, A. C. (1999) Regulation ofGi by the CB1 cannabinoid receptor C-terminal juxtamembrane region. Structural requirements determined by peptide analysis. Biochemistry 38, 3447-3455
    • (1999) Biochemistry , vol.38 , pp. 3447-3455
    • Mukhopadhyay, S.1    Cowsik, S.M.2    Lynn, A.M.3    Welsh, W.J.4    Howlett, A.C.5
  • 86
    • 0242552831 scopus 로고    scopus 로고
    • The [35S] GTPγS binding assay. Approaches and applications in pharmacology
    • Harrison, C., and Traynor, J. R. (2003) The [35S]GTPγS binding assay. Approaches and applications in pharmacology. Life Sci. 74, 489-508
    • (2003) Life Sci , vol.74 , pp. 489-508
    • Harrison, C.1    Traynor, J.R.2
  • 87
    • 41149089767 scopus 로고    scopus 로고
    • Mapping the structural requirements in the CB1 cannabinoid receptor transmembrane helix II for signal transduction
    • Kapur, A., Samaniego, P., Thakur, G. A., Makriyannis, A., and Abood, M. E. (2008) Mapping the structural requirements in the CB1 cannabinoid receptor transmembrane helix II for signal transduction. J. Pharmacol. Exp. Ther. 325, 341-348
    • (2008) J. Pharmacol. Exp. Ther , vol.325 , pp. 341-348
    • Kapur, A.1    Samaniego, P.2    Thakur, G.A.3    Makriyannis, A.4    Abood, M.E.5
  • 88
    • 78650369170 scopus 로고    scopus 로고
    • Probing the structural determinants for the function of intracellular loop 2 in structurally cognate G-protein-coupled receptors
    • Shan, J., Weinstein, H., and Mehler, E. L. (2010) Probing the structural determinants for the function of intracellular loop 2 in structurally cognate G-protein-coupled receptors. Biochemistry 49, 10691-10701
    • (2010) Biochemistry , vol.49 , pp. 10691-10701
    • Shan, J.1    Weinstein, H.2    Mehler, E.L.3
  • 91
    • 33748803064 scopus 로고    scopus 로고
    • The effects of chargeneutralizing mutation D6.30N on the functions of CB1 and CB2 cannabinoid receptors
    • Nebane, N. M., Kellie, B., and Song, Z. H. (2006) The effects of chargeneutralizing mutation D6.30N on the functions of CB1 and CB2 cannabinoid receptors. FEBS Lett. 580, 5392-5398
    • (2006) FEBS Lett , vol.580 , pp. 5392-5398
    • Nebane, N.M.1    Kellie, B.2    Song, Z.H.3
  • 94
    • 77957055780 scopus 로고
    • Integrated methods for modeling G-protein coupled receptors
    • (Conn, P. M., and Sealfon, S. C., eds), Academic Press, Inc., San Francisco
    • Ballesteros, J. A., and Weinstein, H. (1995). Integrated methods for modeling G-protein coupled receptors. in Methods in Neuroscience (Conn, P. M., and Sealfon, S. C., eds) pp. 366-428, Academic Press, Inc., San Francisco
    • (1995) Methods in Neuroscience , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 95
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee. A novel method for fast and accurate multiple sequence alignment
    • Notredame, C., Higgins, D. G., and Heringa, J. (2000) T-Coffee. A novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302, 205-217
    • (2000) J. Mol. Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3


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