Cited by 105Receptor Mechanisms and SignalingProtein Structure and DynamicsProtein Kinase Regulation and GTPase Signaling

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Conformational Flexibility and Structural Dynamics in GPCR-Mediated G Protein Activation: A Perspective

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Preininger, Anita M., Meiler, Jens, Hamm, Heidi E.·2013·Journal of Molecular Biology

DOI 10.1016/j.jmb.2013.04.011PMC PMC3686903

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Abstract

Structure and dynamics of G proteins and their cognate receptors, both alone and in complex, are becoming increasingly accessible to experimental techniques. Understanding the conformational changes and timelines that govern these changes can lead to new insights into the processes of ligand binding and associated G protein activation. Experimental systems may involve the use of, or otherwise stabilize, non-native environments. This can complicate our understanding of structural and dynamic features of processes such as the ionic lock, tryptophan toggle, and G protein flexibility. While elements in the receptor's transmembrane helices and the C-terminal α5 helix of Gα undergo well-defined structural changes, regions subject to conformational flexibility may be important in fine-tuning the interactions between activated receptors and G proteins. The pairing of computational and experimental approaches will continue to provide powerful tools to probe the conformation and dynamics of receptor-mediated G protein activation.

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Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor
Palczewski, K., Kumasaka, T., Hori, T., Behnke, C. A., Motoshima, H., Fox, B. A., Trong, I. L., Teller, D. C., Okada, T., Stenkamp, R. E., et al. (2000) · Science · doi:10.1126/science.289.5480.739 · Cited by 5,637
Crystal structure of the β2 adrenergic receptor–Gs protein complex
Rasmussen, S. G. F., DeVree, B. T., Zou, Y., Kruse, A. C., Chung, K. Y., Kobilka, T. S., Thian, F. S., Chae, P. S., Pardon, E., Calinski, D., et al. (2011) · Nature · doi:10.1038/nature10361 · Cited by 3,009
Crystal structure of the human β2 adrenergic G-protein-coupled receptor
Rasmussen, S. G. F., Choi, H., Rosenbaum, D. M., Kobilka, T. S., Thian, F. S., Edwards, P. C., Burghammer, M. C., Ratnala, V. R. P., Sanishvili, R., Fischetti, R. F., et al. (2007) · Nature · doi:10.1038/nature06325 · Cited by 1,935
The 2.6 Angstrom Crystal Structure of a Human A 2A Adenosine Receptor Bound to an Antagonist
Jaakola, V., Griffith, M. T., Hanson, M. A., Cherezov, V., Chien, E. Y. T., Lane, J. R., IJzerman, A. P., & Stevens, R. C. (2008) · Science · doi:10.1126/science.1164772 · Cited by 1,786
Structure of a nanobody-stabilized active state of the β2 adrenoceptor
Rasmussen, S. G. F., Choi, H., Fung, J. J., Pardon, E., Casarosa, P., Chae, P. S., DeVree, B. T., Rosenbaum, D. M., Thian, F. S., Kobilka, T. S., et al. (2011) · Nature · doi:10.1038/nature09648 · Cited by 1,709
Molecular signatures of G-protein-coupled receptors
Venkatakrishnan, A., Deupí, X., Lebon, G., Tate, C. G., Schertler, G. F. X., & Babu, M. M. (2013) · Nature · doi:10.1038/nature11896 · Cited by 1,534
Structure of a β1-adrenergic G-protein-coupled receptor
Warne, T., Serrano‐Vega, M. J., Baker, J. G., Moukhametzianov, R., Edwards, P. C., Henderson, R. A., Leslie, A. G. W., Tate, C. G., & Schertler, G. F. X. (2008) · Nature · doi:10.1038/nature07101 · Cited by 1,377
Crystal structure of opsin in its G-protein-interacting conformation
Scheerer, P., Park, J. H., Hildebrand, P. W., Kim, Y. J., Krauß, N., Choe, H.-W., Hofmann, K. P., & Ernst, O. P. (2008) · Nature · doi:10.1038/nature07330 · Cited by 1,059
Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions
Liu, W., Chun, E., Thompson, A. A., Chubukov, P., Xu, F., Katritch, V., Han, G. W., Roth, C., Heitman, L. H., IJzerman, A. P., et al. (2012) · Science · doi:10.1126/science.1219218 · Cited by 952
Crystal structure of the ligand-free G-protein-coupled receptor opsin
Park, J. H., Scheerer, P., Hofmann, K. P., Choe, H., & Ernst, O. P. (2008) · Nature · doi:10.1038/nature07063 · Cited by 908
Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation
Lebon, G., Warne, T., Edwards, P. C., Bennett, K. A., Langmead, C. J., Leslie, A. G. W., & Tate, C. G. (2011) · Nature · doi:10.1038/nature10136 · Cited by 892
Structure of an Agonist-Bound Human A 2A Adenosine Receptor
Xu, F., Wu, H., Katritch, V., Han, G. W., Jacobson, K. A., Gao, Z., Cherezov, V., & Stevens, R. C. (2011) · Science · doi:10.1126/science.1202793 · Cited by 820
Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis
Coleman, D. E., Berghuis, A. M., Lee, E., Linder, M., Gilman, A. G., & Sprang (1994) · Science · doi:10.1126/science.8073283 · Cited by 815
The Dynamic Process of β2-Adrenergic Receptor Activation
Nygaard, R., Zou, Y., Dror, R. O., Mildorf, T. J., Arlow, D. H., Manglik, A., Pan, A. C., Liu, C. W., Fung, J. J., Bokoch, M. P., et al. (2013) · Cell · doi:10.1016/j.cell.2013.01.008 · Cited by 815
The 2.2 Å crystal structure of transducin-α complexed with GTPγS
Noel, J. P., Hamm, H. E., & Sigler, P. B. (1993) · Nature · doi:10.1038/366654a0 · Cited by 803
Self-citation
Crystal Structure of the Catalytic Domains of Adenylyl Cyclase in a Complex with G sα ·GTPγS
Tesmer, J. J. G., Sunahara, R. K., Gilman, A. G., & Sprang, S. R. (1997) · Science · doi:10.1126/science.278.5345.1907 · Cited by 792
Structure and function of an irreversible agonist-β2 adrenoceptor complex
Rosenbaum, D. M., Zhang, C., Lyons, J. A., Holl, R., Aragão, D., Arlow, D. H., Rasmussen, S. G. F., Choi, H., DeVree, B. T., Sunahara, R. K., et al. (2011) · Nature · doi:10.1038/nature09665 · Cited by 771
Biased Signaling Pathways in β 2 -Adrenergic Receptor Characterized by 19 F-NMR
Liu, J. J., Horst, R., Katritch, V., Stevens, R. C., & Wüthrich, K. (2012) · Science · doi:10.1126/science.1215802 · Cited by 706
Conformational complexity of G-protein-coupled receptors
Kobilka, B. K., & Deupí, X. (2007) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2007.06.003 · Cited by 694
Crystal structure of metarhodopsin II
Choe, H.-W., Kim, Y. J., Park, J. H., Morizumi, T., Pai, E. F., Krauß, N., Hofmann, K. P., Scheerer, P., & Ernst, O. P. (2011) · Nature · doi:10.1038/nature09789 · Cited by 663
Activation mechanism of the β 2 -adrenergic receptor
Dror, R. O., Arlow, D. H., Maragakis, P., Mildorf, T. J., Pan, A. C., Xu, H., Borhani, D. W., & Shaw, D. E. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110499108 · Cited by 629
The structural basis for agonist and partial agonist action on a β1-adrenergic receptor
Warne, T., Moukhametzianov, R., Baker, J. G., Nehmé, R., Edwards, P. C., Leslie, A. G. W., Schertler, G. F. X., & Tate, C. G. (2011) · Nature · doi:10.1038/nature09746 · Cited by 625
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. F., Shi, L., Gether, U., & Javitch, J. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103747200 · Cited by 619
Site of G Protein Binding to Rhodopsin Mapped with Synthetic Peptides from the α Subunit
Hamm, H. E., Deretic, D., Arendt, A., Hargrave, P. A., Koenig, B. W., & Hofmann, K. P. (1988) · Science · doi:10.1126/science.3136547 · Cited by 498
Self-citation
The structural basis of agonist-induced activation in constitutively active rhodopsin
Standfuss, J., Edwards, P. C., D’Antona, A. M., Fransen, M. P., Xie, G., Oprian, D. D., & Schertler, G. F. X. (2011) · Nature · doi:10.1038/nature09795 · Cited by 481
The Highly Conserved DRY Motif of Class A G Protein-Coupled Receptors: Beyond the Ground State
Rovati, G. E., Capra, V., & Neubig, R. R. (2007) · Molecular Pharmacology · doi:10.1124/mol.106.029470 · Cited by 392
Conformational changes in the G protein Gs induced by the β2 adrenergic receptor
Chung, K. Y., Rasmussen, S. G. F., Liu, T., Li, S., DeVree, B. T., Chae, P. S., Calinski, D. M., Kobilka, B. K., Woods, V. L., & Sunahara, R. K. (2011) · Nature · doi:10.1038/nature10488 · Cited by 368
Conserved Binding Mode of Human β2Adrenergic Receptor Inverse Agonists and Antagonist Revealed by X-ray Crystallography
Wacker, D., Fenalti, G., Brown, M. A., Katritch, V., Abagyan, R. A., Cherezov, V., & Stevens, R. C. (2010) · Journal of the American Chemical Society · doi:10.1021/ja105108q · Cited by 358
Identification of two distinct inactive conformations of the β 2 -adrenergic receptor reconciles structural and biochemical observations
Dror, R. O., Arlow, D. H., Borhani, D. W., Jensen, M. Ø., Piana, S., & Shaw, D. E. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811065106 · Cited by 307
Structural flexibility of the Gαs α-helical domain in the β 2 -adrenoceptor Gs complex
Westfield, G., Rasmussen, S. G. F., Su, M., Dutta, S., DeVree, B. T., Chung, K. Y., Calinski, D. M., Vélez-Ruiz, G. A., Oleskie, A. N., Pardon, E., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113645108 · Cited by 230
Hydrophobic amino acid in the i2 loop plays a key role in receptor-G protein coupling.
Moro, O., Lameh, J., Högger, P., & Sadée, W. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41524-4 · Cited by 218
Local peptide movement in the photoreaction intermediate of rhodopsin
Nakamichi, H., & Okada, T. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601765103 · Cited by 204
A Lipid Pathway for Ligand Binding Is Necessary for a Cannabinoid G Protein-coupled Receptor
Hurst, D. P., Grossfield, A. M., Lynch, D. L., Feller, S. E., Romo, T. D., Gawrisch, K., Pitman, M. C., & Reggio, P. H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.041590 · Cited by 203
Mechanism of the receptor-catalyzed activation of heterotrimeric G proteins
Oldham, W. M., Eps, N. V., Preininger, A. M., Hubbell, W. L., & Hamm, H. E. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1129 · Cited by 179
Self-citation
Interaction of a G protein with an activated receptor opens the interdomain interface in the alpha subunit
Eps, N. V., Preininger, A. M., Alexander, N. S., Kaya, A. İ., Meier, S., Meiler, J., Hamm, H. E., & Hubbell, W. L. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1105810108 · Cited by 162
Self-citation
Critical Role for the Second Extracellular Loop in the Binding of Both Orthosteric and Allosteric G Protein-coupled Receptor Ligands
Avlani, V. A., Gregory, K. J., Morton, C. J., Parker, M. W., Sexton, P. M., & Christopoulos, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702311200 · Cited by 157
Cholesterol increases kinetic, energetic, and mechanical stability of the human β 2 -adrenergic receptor
Zocher, M., Zhang, C., Rasmussen, S. G. F., Kobilka, B. K., & Müller, D. J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1210373109 · Cited by 156
Potent Peptide Analogues of a G Protein Receptor-binding Region Obtained with a Combinatorial Library
Martin, E. L., Rens‐Domiano, S., Schatz, P. J., & Hamm, H. E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.1.361 · Cited by 155
Self-citation
Ligand-Dependent Perturbation of the Conformational Ensemble for the GPCR β2 Adrenergic Receptor Revealed by HDX
West, G. M., Chien, E. Y. T., Katritch, V., Gatchalian, J., Chalmers, M. J., Stevens, R. C., & Griffin, P. R. (2011) · Structure · doi:10.1016/j.str.2011.08.001 · Cited by 143
Internal Hydration Increases during Activation of the G-Protein-Coupled Receptor Rhodopsin
Grossfield, A. M., Pitman, M. C., Feller, S. E., Soubias, O., & Gawrisch, K. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.05.036 · Cited by 141
Role of the Extracellular Loops of G Protein-Coupled Receptors in Ligand Recognition: A Molecular Modeling Study of the Human P2Y1Receptor
Moro, S., Hoffmann, C., & Jacobson, K. A. (1999) · Biochemistry · doi:10.1021/bi982369v · Cited by 129
The Second Intracellular Loop of the m5 Muscarinic Receptor Is the Switch Which Enables G-protein Coupling
Burstein, E. S., Spalding, T. A., & Brann, M. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.38.24322 · Cited by 124
Evaluating Cellular Impedance Assays for Detection of GPCR Pleiotropic Signaling and Functional Selectivity
Peters, M. F., & Scott, C. W. (2009) · SLAS DISCOVERY · doi:10.1177/1087057108330115 · Cited by 121
Mapping of Single Amino Acid Residues Required for Selective Activation of G by the m3 Muscarinic Acetylcholine Receptor
Blin, N., Yun, J. S., & Wess, J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.30.17741 · Cited by 116
Cholesterol heterogeneity in bovine rod outer segment disk membranes
Boesze‐Battaglia, K., Hennessey, T. M., & Albert, A. D. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83162-3 · Cited by 108
Rhodopsin Activation Exposes a Key Hydrophobic Binding Site for the Transducin α-Subunit C Terminus
Janz, J. M., & Farrens, D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402567200 · Cited by 107
Gα Minigenes Expressing C-terminal Peptides Serve as Specific Inhibitors of Thrombin-mediated Endothelial Activation
Gilchrist, A., Vanhauwe, J. F. M., Li, A., Thomas, T. O., Voyno-Yasenetskaya, T., & Hamm, H. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100914200 · Cited by 102
Self-citation
Predictions for Cholesterol Interaction Sites on the A2A Adenosine Receptor
Lee, J. Y., & Lyman, E. R. (2012) · Journal of the American Chemical Society · doi:10.1021/ja307532d · Cited by 98
Ligand-Specific Interactions Modulate Kinetic, Energetic, and Mechanical Properties of the Human β2 Adrenergic Receptor
Zocher, M., Fung, J. J., Kobilka, B. K., & Müller, D. J. (2012) · Structure · doi:10.1016/j.str.2012.05.010 · Cited by 94
Inhibition of inositol phosphate second messenger formation by intracellular loop one of a human calcitonin receptor. Expression and mutational analysis of synthetic receptor genes.
Nussenzveig, D. R., Thaw, C. N., & Gershengorn, M. C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)46903-7 · Cited by 85
Recent progress in the study of G protein-coupled receptors with molecular dynamics computer simulations
Grossfield, A. M. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.03.010 · Cited by 81
The N-terminal Extension of Gαq Is Critical for Constraining the Selectivity of Receptor Coupling
Kostenis, E., Degtyarev, M. Y., Conklin, B. R., & Wess, J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.31.19107 · Cited by 79
Structural Basis for Ligand Binding and Specificity in Adrenergic Receptors: Implications for GPCR-Targeted Drug Discovery
Huber, T., Menon, S. T., & Sakmar, T. P. (2008) · Biochemistry · doi:10.1021/bi800891r · Cited by 75
Structural and dynamical changes in an α-subunit of a heterotrimeric G protein along the activation pathway
Eps, N. V., Oldham, W. M., Hamm, H. E., & Hubbell, W. L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607972103 · Cited by 74
Self-citation
Disease-causing Mutation in GPR54 Reveals the Importance of the Second Intracellular Loop for Class A G-protein-coupled Receptor Function
Wacker, J. L., Feller, D. B., Tang, X.-B., DeFino, M. C., Namkung, Y., Lyssand, J. S., Mhyre, A. J., Tan, X., Jensen, J. B., & Hague, C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805251200 · Cited by 71 · cited 1×
“25 This particular IC2 loop residue has been shown to play an important role in physiology, as an L-to-S mutation in the residue that is homologous to F139 in the GPCR, GPR54, causes idiopathic hypogonadotropic hypogonadism, a disorder associated with delayed puberty and infertility.(64)”
Background
Conformational Dynamics of Activation for the Pentameric Complex of Dimeric G Protein-Coupled Receptor and Heterotrimeric G Protein
Orban, T., Jastrzebska, B., Gupta, S., Wang, B., Miyagi, M., Chance, M. R., & Palczewski, K. (2012) · Structure · doi:10.1016/j.str.2012.03.017 · Cited by 67
Concerted Interconversion between Ionic Lock Substates of the β2 Adrenergic Receptor Revealed by Microsecond Timescale Molecular Dynamics
Romo, T. D., Grossfield, A. M., & Pitman, M. C. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2009.09.046 · Cited by 67
Structural determinants in the second intracellular loop of the human cannabinoid CB1receptor mediate selective coupling to Gsand Gi
Chen, X., Yang, W. J., Fan, Y., Luo, J., Hong, K., Wang, Z., Yan, J., Chen, X., Lu, J., Benovic, J., et al. (2010) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2010.01006.x · Cited by 66
Impact of the DRY Motif and the Missing “Ionic Lock” on Constitutive Activity and G-Protein Coupling of the Human Histamine H4 Receptor
Schneider, E. H., Schnell, D., Straßer, A., Dove, S., & Seifert, R. (2010) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.109.163220 · Cited by 66
Rapid Activation of Transducin by Mutations Distant from the Nucleotide-binding Site
Marin, E. P., Krishna, A. G., & Sakmar, T. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100198200 · Cited by 64
Mutation of tyrosine‐141 inhibits insulin‐promoted tyrosine phosphorylation and increased responsiveness of the human beta 2‐adrenergic receptor.
Valiquette, M., Parent, S., Loisel, T. P., & Bouvier, M. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00241.x · Cited by 59
Single Amino Acid Substitutions and Deletions That Alter the G Protein Coupling Properties of the V2 Vasopressin Receptor Identified in Yeast by Receptor Random Mutagenesis
Erlenbach, I., Kostenis, E., Schmidt, C. L., Gal, C. S., Raufaste, D., Dumont, M. E., Pausch, M. H., & Wess, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103203200 · Cited by 59
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., & Ridge, K. D. (2006) · Biochemistry · doi:10.1021/bi061088h · Cited by 54
The Nucleotide Exchange Factor Ric-8A Is a Chaperone for the Conformationally Dynamic Nucleotide-Free State of Gαi1
Thomas, C. J., Briknarová, K., Hilmer, J. K., Movahed, N., Bothner, B. B., Sumida, J. P., Tall, G. G., & Sprang, S. R. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023197 · Cited by 50
Disruption of the α5 Helix of Transducin Impairs Rhodopsin-Catalyzed Nucleotide Exchange
Marin, E. P., Krishna, A. G., & Sakmar, T. P. (2002) · Biochemistry · doi:10.1021/bi025514k · Cited by 49
A Novel Site on the Gα-protein That Recognizes Heptahelical Receptors
Blahoš, J., Fischer, T., Brabet, I., Stauffer, D., Rovelli, G., Bockaert, J., & Pin, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m004880200 · Cited by 47
Two Amino Acids within the α4 Helix of Gαi1Mediate Coupling with 5-Hydroxytryptamine1BReceptors
Bae, H., Cabrera-Vera, T. M., Depree, K. M., Graber, S. G., & Hamm, H. E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.21.14963 · Cited by 47
Self-citation
From Valleys to Ridges: Exploring the Dynamic Energy Landscape of Single Membrane Proteins
Janovjak, H., Sapra, K. T., Kedrov, A., & Müller, D. J. (2008) · ChemPhysChem · doi:10.1002/cphc.200700662 · Cited by 47
Molecular Dynamics Simulations of the Adenosine A2a Receptor: Structural Stability, Sampling, and Convergence
Ng, H. W., Laughton, C. A., & Doughty, S. W. (2013) · Journal of Chemical Information and Modeling · doi:10.1021/ci300610w · Cited by 47
Structural Evidence for a Sequential Release Mechanism for Activation of Heterotrimeric G Proteins
Kapoor, N., Menon, S. T., Chauhan, R., Sachdev, P., & Sakmar, T. P. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.08.043 · Cited by 47
Molecular Dynamics Simulations of Transducin: Interdomain and Front to Back Communication in Activation and Nucleotide Exchange
Ceruso, M. A., Périole, X., & Weinstein, H. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.064 · Cited by 46
Dynamic Structure of Retinylidene Ligand of Rhodopsin Probed by Molecular Simulations
Lau, P.-W., Grossfield, A. M., Feller, S. E., Pitman, M. C., & Brown, M. F. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.06.047 · Cited by 44
Molecular Aspects of Vasopressin Receptor Function
Schöneberg, T., Kostenis, E., Liu, J., Gudermann, T. W., & Wess, J. (1998) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-4871-3_44 · Cited by 37
Conformational Changes Associated with Receptor-stimulated Guanine Nucleotide Exchange in a Heterotrimeric G-protein α-Subunit
Ridge, K. D., Abdulaev, N. G., Zhang, C., Ngo, T., Brabazon, D. M., & Marino, J. P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m509851200 · Cited by 36
Molecular simulations and solid-state NMR investigate dynamical structure in rhodopsin activation
Mertz, B., Владимирович, С. А., Feller, S. E., & Brown, M. F. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.08.003 · Cited by 36
Agonist Dynamics and Conformational Selection during Microsecond Simulations of the A2A Adenosine Receptor
Lee, J. Y., & Lyman, E. R. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.03.061 · Cited by 35
Roles of the Transducin α-Subunit α4-Helix/α4-β6 Loop in the Receptor and Effector Interactions
Natochin, M., Granovsky, A. E., Muradov, K. G., & Artemyev, N. O. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.12.7865 · Cited by 31
A Concerted Mechanism for Opening the GDP Binding Pocket and Release of the Nucleotide in Hetero-Trimeric G-Proteins
Louet, M., Pérahia, D., Martínez, J., & Floquet, N. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.05.034 · Cited by 29
The metabotropic glutamate receptors: their second intracellular loop plays a critical role in the G-protein coupling specificity
Pin, J., Gomeza, J., Joly, C., & Bockaert, J. (1995) · Biochemical Society Transactions · doi:10.1042/bst0230091 · Cited by 28
Predictions for Cholesterol Interaction Sites on the A2A Adenosine Receptor
Lee, J. Y., & Lyman, E. R. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2012.11.2967 · Cited by 27
Helix Dipole Movement and Conformational Variability Contribute to Allosteric GDP Release in GαiSubunits,
Preininger, A. M., Funk, M. A., Oldham, W. M., Meier, S., Johnston, C. A., Adhikary, S., Kimple, A. J., Siderovski, D. P., Hamm, H. E., & Iverson, T. M. (2009) · Biochemistry · doi:10.1021/bi801853a · Cited by 23
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Orban, 2013, Conformational dynamics of activation for the pentameric complex of dimeric G protein-coupled receptor and heterotrimeric G protein, Structure, 20, 826, 10.1016/j.str.2012.03.017 · DOI · Paper page

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Authors: Preininger, A. M., Meiler, J., & Hamm, H. E.
Affiliations: Vanderbilt University Medical Center (US)
Vanderbilt University (US)
Corresponding author: Preininger, Anita M.
ORCID: Preininger, Anita M.
Meiler, Jens
Hamm, Heidi E.
Venue: Journal of Molecular Biology
Publisher: Elsevier BV
Published: 2013-07
Volume: 425
Issue: 13
Pages: 2288-2298
ISSN: 0022-2836 (ISSN-L)
DOI: 10.1016/j.jmb.2013.04.011
PMC: PMC3686903
OpenAlex: W2064856742
Cited by: 104
References: 90
Citations by year: 2026: 5 · 2025: 5 · 2024: 3 · 2023: 7 · 2022: 6 · 2021: 5 · 2020: 5 · 2019: 11 · 2018: 9 · 2017: 5 · 2016: 6 · 2015: 15 · 2014: 17 · 2013: 5
FWCI: 1.35
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Journal of Molecular Biology (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute of Mental Health (MH090192, R01MH090192)
National Eye Institute (EY006062, R01EY006062)
National Institute of General Medical Sciences (R01GM095633, R01GM099842, R01GM080403, GM 080403, GM099842, GM095633)
National Institute of Diabetes and Digestive and Kidney Diseases (R01DK097376)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords: G protein-coupled receptors, G protein activation, conformational flexibility, structural dynamics, ligand binding, ionic lock, transmembrane helices, receptor-G protein interaction
MeSH terms: Allosteric Regulation, Models, Molecular, Protein Conformation, Signal Transduction, Crystallography, X-Ray, GTP-Binding Proteins, Receptors, G-Protein-Coupled, Molecular Dynamics Simulation

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Conformational Flexibility and Structural Dynamics in GPCR-Mediated G Protein Activation: A Perspective

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