Crystal structure of the β2 adrenergic receptor–Gs protein complex (original) (raw)

• Dixon, R. A. et al. Cloning of the gene and cDNA for mammalian β-adrenergic receptor and homology with rhodopsin. Nature 321, 75–79 (1986)
  Article ADS CAS Google Scholar
• Rasmussen, S. G. et al. Crystal structure of the human β2 adrenergic G-protein-coupled receptor. Nature 450, 383–387 (2007)
  Article ADS CAS Google Scholar
• Rosenbaum, D. M. et al. GPCR engineering yields high-resolution structural insights into β2-adrenergic receptor function. Science 318, 1266–1273 (2007)
  Article ADS CAS Google Scholar
• Lefkowitz, R. J. Seven transmembrane receptors: something old, something new. Acta Physiol. (Oxf.) 190, 9–19 (2007)
  Article CAS Google Scholar
• Brandt, D. R., Asano, T., Pedersen, S. E. & Ross, E. M. Reconstitution of catecholamine-stimulated guanosinetriphosphatase activity. Biochemistry 22, 4357–4362 (1983)
  Article CAS Google Scholar
• Cerione, R. A. et al. The mammalian β2-adrenergic receptor: reconstitution of functional interactions between pure receptor and pure stimulatory nucleotide binding protein of the adenylate cyclase system. Biochemistry 23, 4519–4525 (1984)
  Article CAS Google Scholar
• Ross, E. M., Maguire, M. E., Sturgill, T. W., Biltonen, R. L. & Gilman, A. G. Relationship between the β-adrenergic receptor and adenylate cyclase. Studies of ligand binding and enzyme activity in purified membranes of S49 lymphoma cells. J. Biol. Chem. 252, 5761–5775 (1977)
  CAS PubMed Google Scholar
• De Lean, A., Stadel, J. M. & Lefkowitz, R. J. 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)
  CAS Google Scholar
• Fredriksson, R., Lagerstrom, M. C., Lundin, L. G. & Schioth, H. B. 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)
  Article CAS Google Scholar
• Azzi, M. et al. β-arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G protein-coupled receptors. Proc. Natl Acad. Sci. USA 100, 11406–11411 (2003)
  Article ADS CAS Google Scholar
• Lefkowitz, R. J. & Shenoy, S. K. Transduction of receptor signals by β-arrestins. Science 308, 512–517 (2005)
  Article ADS CAS Google Scholar
• Rasmussen, S. G. et al. Structure of a nanobody-stabilized active state of the β2 adrenoceptor. Nature 469, 175–180 (2011)
  Article ADS CAS Google Scholar
• Chae, P. S. et al. Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins. Nature Methods 7, 1003–1008 (2010)
  Article CAS Google Scholar
• Sprang, S. R. G protein mechanisms: insights from structural analysis. Annu. Rev. Biochem. 66, 639–678 (1997)
  Article CAS Google Scholar
• Misquitta, L. V. et al. Membrane protein crystallization in lipidic mesophases with tailored bilayers. Structure 12, 2113–2124 (2004)
  Article CAS Google Scholar
• Domanska, K. et al. Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic β2-microglobulin variant. Proc. Natl Acad. Sci. USA 108, 1314–1319 (2011)
  Article ADS CAS Google Scholar
• Warne, T. et al. Structure of a β1-adrenergic G-protein-coupled receptor. Nature 454, 486–491 (2008)
  Article ADS CAS Google Scholar
• Hofmann, K. P. et al. A G protein-coupled receptor at work: the rhodopsin model. Trends Biochem. Sci. 34, 540–552 (2009)
  Article CAS Google Scholar
• Moro, O., Lameh, J., Hogger, P. & Sadee, W. Hydrophobic amino acid in the i2 loop plays a key role in receptor-G protein coupling. J. Biol. Chem. 268, 22273–22276 (1993)
  CAS PubMed Google Scholar
• Baltensperger, K. et al. The β-adrenergic receptor is a substrate for the insulin receptor tyrosine kinase. J. Biol. Chem. 271, 1061–1064 (1996)
  Article CAS Google Scholar
• Jastrzebska, B., Tsybovsky, Y. & Palczewski, K. Complexes between photoactivated rhodopsin and transducin: progress and questions. Biochem. J. 428, 1–10 (2010)
  Article CAS Google Scholar
• Johnston, C. A. & Siderovski, D. P. Receptor-mediated activation of heterotrimeric G-proteins: current structural insights. Mol. Pharmacol. 72, 219–230 (2007)
  Article CAS Google Scholar
• Breitwieser, G. E. G protein-coupled receptor oligomerization: implications for G protein activation and cell signaling. Circ. Res. 94, 17–27 (2004)
  Article CAS Google Scholar
• Banères, J. L. & Parello, J. Structure-based analysis of GPCR function: evidence for a novel pentameric assembly between the dimeric leukotriene B4 receptor BLT1 and the G-protein. J. Mol. Biol. 329, 815–829 (2003)
  Article Google Scholar
• Angers, S., Salahpour, A. & Bouvier, M. Dimerization: an emerging concept for G protein-coupled receptor ontogeny and function. Annu. Rev. Pharmacol. Toxicol. 42, 409–435 (2002)
  Article CAS Google Scholar
• Sunahara, R. K., Tesmer, J. J., Gilman, A. G. & Sprang, S. R. Crystal structure of the adenylyl cyclase activator Gsα . Science 278, 1943–1947 (1997)
  Article ADS CAS Google Scholar
• Van Eps, N. et al. Interaction of a G protein with an activated receptor opens the interdomain interface in the α subunit. Proc. Natl Acad. Sci. USA 108, 9420–9424 (2011)
  Article ADS CAS Google Scholar
• Markby, D. W., Onrust, R. & Bourne, H. R. Separate GTP binding and GTPase activating domains of a Gα subunit. Science 262, 1895–1901 (1993)
  Article ADS CAS Google Scholar
• Conklin, B. R. & Bourne, H. R. Structural elements of Gα subunits that interact with Gβγ, receptors, and effectors. Cell 73, 631–641 (1993)
  Article CAS Google Scholar
• Oldham, W. M. & Hamm, H. E. Heterotrimeric G protein activation by G-protein-coupled receptors. Nature Rev. Mol. Cell Biol. 9, 60–71 (2008)
  Article CAS Google Scholar
• Wall, M. A. et al. The structure of the G protein heterotrimer Gi_α_1 β 1 γ 2 . Cell 83, 1047–1058 (1995)
  Article CAS Google Scholar
• Choe, H. W. et al. Crystal structure of metarhodopsin II. Nature 471, 651–655 (2011)
  Article ADS CAS Google Scholar
• Standfuss, J. et al. The structural basis of agonist-induced activation in constitutively active rhodopsin. Nature 471, 656–660 (2011)
  Article ADS CAS Google Scholar
• Westfield, G. et al. Structurall flexibility of the Gαs α-helical domain in the β2-adrenoceptor Gs complex. Proc. Nati Acad. Sci. USA 10.1073/pnas.1113645108 (in the press)
• Chung, K. Y. et al. β2 adrenergic receptor-induced conformational changes in the heterotrimeric G protein Gs. Nature 10.1038/nature10488 (this issue)
• Kobilka, B. K. Amino and carboxyl terminal modifications to facilitate the production and purification of a G protein-coupled receptor. Anal. Biochem. 231, 269–271 (1995)
  Article CAS Google Scholar
• Whorton, M. R. et al. A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein. Proc. Natl Acad. Sci. USA 104, 7682–7687 (2007)
  Article ADS CAS Google Scholar
• Caffrey, M. & Cherezov, V. Crystallizing membrane proteins using lipidic mesophases. Nature Protocols 4, 706–731 (2009)
  Article CAS Google Scholar
• Rosenbaum, D. M. et al. Structure and function of an irreversible agonist-β2 adrenoceptor complex. Nature 469, 236–240 (2011)
  Article ADS CAS Google Scholar
• Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307–326 (1997)
  Article CAS Google Scholar
• Strong, M. et al. Toward the structural genomics of complexes: crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis . Proc. Natl Acad. Sci. USA 103, 8060–8065 (2006)
  Article ADS CAS Google Scholar
• McCoy, A. J. Solving structures of protein complexes by molecular replacement with Phaser . Acta Crystallogr. D 63, 32–41 (2007)
  Article CAS Google Scholar
• McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Cryst. 40, 658–674 (2007)
  Article CAS Google Scholar
• Afonine, P. V., Grosse-Kunstleve, R. W. & Adams, P. D. A robust bulk-solvent correction and anisotropic scaling procedure. Acta Crystallogr. D 61, 850–855 (2005)
  Article Google Scholar
• Blanc, E. et al. Refinement of severely incomplete structures with maximum likelihood in BUSTER-TNT . Acta Crystallogr. D 60, 2210–2221 (2004)
  Article CAS Google Scholar
• Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126–2132 (2004)
  Article Google Scholar
• Schröder, G. F., Levitt, M. & Brunger, A. T. Super-resolution biomolecular crystallography with low-resolution data. Nature 464, 1218–1222 (2010)
  Article ADS Google Scholar
• Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D 66, 12–21 (2010)
  Article CAS Google Scholar
• Swaminath, G., Steenhuis, J., Kobilka, B. & Lee, T. W. Allosteric modulation of β2-adrenergic receptor by Zn2+ . Mol. Pharmacol. 61, 65–72 (2002)
  Article CAS Google Scholar