Structure of class B GPCR corticotropin-releasing factor receptor 1 (original) (raw)

• Gether, U. Uncovering molecular mechanisms involved in activation of G protein-coupled receptors. Endocr. Rev. 21, 90–113 (2000)
  Article CAS Google Scholar
• Lagerström, M. C. & Schiöth, H. B. Structural diversity of G protein-coupled receptors and significance for drug discovery. Nature Rev. Drug Discov. 7, 339–357 (2008)
  Article Google Scholar
• Venkatakrishnan, A. J. et al. Molecular signatures of G-protein-coupled receptors. Nature 494, 185–194 (2013)
  Article ADS CAS Google Scholar
• Bhavsar, S., Mudaliar, S. & Cherrington, A. Evolution of exenatide as a diabetes therapeutic. Curr. Diabetes Rev. 9, 161–193 (2013)
  PubMed PubMed Central Google Scholar
• Berg, C., Neumeyer, K. & Kirkpatrick, P. Teriparatide. Nature Rev. Drug Discov. 2, 257–258 (2003)
  Article CAS Google Scholar
• Rosenbaum, D. M., Rasmussen, S. G. F. & Kobilka, B. K. The structure and function of G-protein-coupled receptors. Nature 459, 356–363 (2009)
  Article ADS CAS Google Scholar
• Wang, C. et al. Structure of the human smoothened receptor bound to an antitumour agent. Nature 497, 338–343 (2013)
  Article ADS CAS Google Scholar
• Congreve, M., Langmead, C. & Marshall, F. H. The use of GPCR structures in drug design. Adv. Pharmacol. 62, 1–36 (2011)
  Article CAS Google Scholar
• Pioszak, A. A., Parker, N. R., Suino-Powell, K. & Xu, H. E. Molecular recognition of corticotropin-releasing factor by its G-protein-coupled receptor CRFR1. J. Biol. Chem. 283, 32900–32912 (2008)
  Article CAS Google Scholar
• Grace, C. R. R. et al. NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor. Proc. Natl Acad. Sci. USA 101, 12836–12841 (2004)
  Article ADS CAS Google Scholar
• Runge, S., Thøgersen, H., Madsen, K., Lau, J. & Rudolph, R. Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain. J. Biol. Chem. 283, 11340–11347 (2008)
  Article CAS Google Scholar
• Pioszak, A. A. & Xu, H. E. Molecular recognition of parathyroid hormone by its G protein-coupled receptor. Proc. Natl Acad. Sci. USA 105, 5034–5039 (2008)
  Article ADS CAS Google Scholar
• ter Haar, E. et al. Crystal structure of the ectodomain complex of the CGRP receptor, a class-B GPCR, reveals the site of drug antagonism. Structure 18, 1083–1093 (2010)
  Article CAS Google Scholar
• Kumar, S., Pioszak, A., Zhang, C., Swaminathan, K. & Xu, H. E. Crystal structure of the PAC1R extracellular domain unifies a consensus fold for hormone recognition by class B G-protein coupled receptors. PLoS ONE 6, e19682 (2011)
  Article ADS CAS Google Scholar
• Koth, C. M. et al. Molecular basis for negative regulation of the glucagon receptor. Proc. Natl Acad. Sci. USA 109, 14393–14398 (2012)
  Article ADS CAS Google Scholar
• Perrin, M. H. & Vale, W. W. Corticotropin releasing factor receptors and their ligand family. Ann. NY Acad. Sci. 885, 312–328 (1999)
  Article ADS CAS Google Scholar
• Bale, T. L. & Vale, W. W. CRF and CRF receptors: role in stress responsivity and other behaviors. Annu. Rev. Pharmacol. Toxicol. 44, 525–557 (2004)
  Article CAS Google Scholar
• Hemley, C. F., McCluskey, A. & Keller, P. A. Corticotropin releasing hormone–a GPCR drug target. Curr. Drug Targets 8, 105–115 (2007)
  Article CAS Google Scholar
• Chen, Y. L. et al. 2-aryloxy-4-alkylaminopyridines: discovery of novel corticotropin-releasing factor 1 antagonists. J. Med. Chem. 51, 1385–1392 (2008)
  Article CAS Google Scholar
• Hoare, S. R. et al. Allosteric ligands for the corticotropin releasing factor type 1 receptor modulate conformational states involved in receptor activation. Mol. Pharmacol. 73, 1371–1380 (2008)
  Article CAS Google Scholar
• Zorrilla, E. P. & Koob, G. F. Progress in corticotropin-releasing factor-1 antagonist development. Drug Discov. Today 15, 371–383 (2010)
  Article CAS Google Scholar
• Serrano-Vega, M. J., Magnani, F., Shibata, Y. & Tate, C. G. Conformational thermostabilization of the β1-adrenergic receptor in a detergent-resistant form. Proc. Natl Acad. Sci. USA 105, 877–882 (2008)
  Article ADS CAS Google Scholar
• Shibata, Y. et al. Thermostabilization of the neurotensin receptor NTS1. J. Mol. Biol. 390, 262–277 (2009)
  Article CAS Google Scholar
• Lebon, G., Bennett, K., Jazayeri, A. & Tate, C. G. Thermostabilisation of an agonist-bound conformation of the human adenosine A2A receptor. J. Mol. Biol. 409, 298–310 (2011)
  Article CAS Google Scholar
• Piserchio, A., Bisello, A., Rosenblatt, M., Chorev, M. & Mierke, D. F. Characterization of parathyroid hormone/receptor interactions: structure of the first extracellular loop. Biochemistry 39, 8153–8160 (2000)
  Article CAS Google Scholar
• Wootten, D., Simms, J., Miller, L. J., Christopoulos, A. & Sexton, P. M. Polar transmembrane interactions drive formation of ligand-specific and signal pathway-biased family B G protein-coupled receptor conformations. Proc. Natl Acad. Sci. USA 110, 5211–5216 (2013)
  Article ADS CAS Google Scholar
• Katritch, V., Cherezov, V. & Stevens, R. C. Diversity and modularity of G protein-coupled receptor structures. Trends Pharmacol. Sci. 33, 17–27 (2012)
  Article CAS Google Scholar
• Mann, R. J., Al-Sabah, S., De Maturana, R. L., Sinfield, J. K. & Donnelly, D. Functional coupling of Cys-226 and Cys-296 in the glucagon-like peptide-1 (GLP-1) receptor indicates a disulfide bond that is close to the activation pocket. Peptides 31, 2289–2293 (2010)
  Article CAS Google Scholar
• Chien, E. Y. T. et al. Structure of the human dopamine D3 receptor in complex with a D2/D3 selective antagonist. Science 330, 1091–1095 (2010)
  Article ADS CAS Google Scholar
• Ballesteros, J. A. & Weinstein, H. Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors. Methods Neurosci. 25, 366–428 (1995)
  Article CAS Google Scholar
• Rasmussen, S. G. F. et al. Crystal structure of the β2 adrenergic receptor–Gs protein complex. Nature 477, 549–555 (2011)
  Article ADS CAS Google Scholar
• Schipani, E., Kruse, K. & Jüppner, H. A constitutively active mutant PTH-PTHrP receptor in Jansen-type metaphyseal chondrodysplasia. Science 268, 98–100 (1995)
  Article ADS CAS Google Scholar
• Heller, R. S., Kieffer, T. J. & Habener, J. F. Point mutations in the first and third intracellular loops of the glucagon-like peptide-1 receptor alter intracellular signaling. Biochem. Biophys. Res. Commun. 223, 624–632 (1996)
  Article CAS Google Scholar
• Hjorth, S. A., Orskov, C. & Schwartz, T. W. Constitutive activity of glucagon receptor mutants. Mol. Endocrinol. 12, 78–86 (1998)
  Article CAS Google Scholar
• Vohra, S. et al. Similarity between class A and class B G-protein-coupled receptors exemplified through calcitonin gene-related peptide receptor modelling and mutagenesis studies. J. R. Soc. Interface 10, 20120846 (2013)
  Article Google Scholar
• Hoare, S. R. J. et al. Single amino acid residue determinants of non-peptide antagonist binding to the corticotropin-releasing factor1 (CRF1) receptor. Biochem. Pharmacol. 72, 244–255 (2006)
  Article CAS Google Scholar
• Gardella, T. J., Luck, M. D., Fan, M. H. & Lee, C. Transmembrane residues of the parathyroid hormone (PTH)/PTH-related peptide receptor that specifically affect binding and signaling by agonist ligands. J. Biol. Chem. 271, 12820–12825 (1996)
  Article CAS Google Scholar
• Conner, A. C. et al. A key role for transmembrane prolines in calcitonin receptor-like receptor agonist binding and signalling: implications for family B G-protein-coupled receptors. Mol. Pharmacol. 67, 20–31 (2005)
  Article CAS Google Scholar
• Chugunov, A. O. et al. Evidence that interaction between conserved residues in transmembrane helices 2, 3, and 7 are crucial for human VPAC1 receptor activation. Mol. Pharmacol. 78, 394–401 (2010)
  Article CAS Google Scholar
• Ganguli, S. C. et al. Protean effects of a natural peptide agonist of the G protein-coupled secretin receptor demonstrated by receptor mutagenesis. J. Pharmacol. Exp. Ther. 286, 593–598 (1998)
  CAS PubMed Google Scholar
• Robertson, N. et al. The properties of thermostabilised G protein-coupled receptors (StaRs) and their use in drug discovery. Neuropharmacology 60, 36–44 (2011)
  Article CAS Google Scholar
• Söding, J. Protein homology detection by HMM–HMM comparison. Bioinformatics 21, 951–960 (2005)
  Article Google Scholar
• Krogh, A., Larsson, B., von Heijne, G. & Sonnhammer, E. L. L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305, 567–580 (2001)
  Article CAS Google Scholar
• Kawate, T. & Gouaux, E. Fluorescence-detection size-exclusion chromatography for precrystallization screening of integral membrane proteins. Structure 14, 673–681 (2006)
  Article CAS Google Scholar
• Caffrey, M. & Cherezov, V. Crystallizing membrane proteins using lipidic cubic mesophases. Nature Protocols 4, 706–731 (2009)
  Article CAS Google Scholar
• Kabsch, W. XDS. Acta Crystallogr. D 66, 125–132 (2010)
  Article CAS Google Scholar
• Leslie, A. G. W. & Powell, H. R. Processing diffraction data with Mosflm. Evolv. Methods Macromol. Crystallogr. 245, 41–51 (2007)
  Article Google Scholar
• Winn, M. D. et al. Overview of the CCP4 suite and current developments. Acta Crystallogr. D 67, 235–242 (2011)
  Article CAS Google Scholar
• Hanson, M. A. et al. Crystal structure of a lipid G protein-coupled receptor. Science 335, 851–855 (2012)
  Article ADS CAS Google Scholar
• McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Cryst. 40, 658–674 (2007)
  Article CAS Google Scholar
• Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D 66, 486–501 (2010)
  Article CAS Google Scholar
• Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213–221 (2010)
  Article CAS Google Scholar
• Murshudov, G. N. et al. REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr. D 67, 355–367 (2011)
  Article CAS Google Scholar
• Haddadian, E. J. et al. Automated real-space refinement of protein structures using a realistic backbone move set. Biophys. J. 101, 899–909 (2011)
  Article ADS CAS 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