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Volumn 548, Issue 7668, 2017, Pages 480-484

Mechanism of intracellular allosteric β 2 AR antagonist revealed by X-ray crystal structure

Author keywords

[No Author keywords available]

Indexed keywords

BETA 2 ADRENERGIC RECEPTOR; BETA 2 ADRENERGIC RECEPTOR BLOCKING AGENT; CARAZOLOL; DIPEPTIDE; PROPANOLAMINE DERIVATIVE;

EID: 85028324189     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature23652     Document Type: Article
Times cited : (149)

References (40)
  • 1
    • 85013129683 scopus 로고    scopus 로고
    • Allosteric 'beta-blocker' isolated from a DNA-encoded small molecule library
    • Ahn, S. et al. Allosteric 'beta-blocker' isolated from a DNA-encoded small molecule library. Proc. Natl Acad. Sci. 114, 1708-1713 (2017).
    • (2017) Proc. Natl Acad. Sci. , vol.114 , pp. 1708-1713
    • Ahn, S.1
  • 2
    • 84889564886 scopus 로고    scopus 로고
    • Activation and allosteric modulation of a muscarinic acetylcholine receptor
    • Kruse, A. C. et al. Activation and allosteric modulation of a muscarinic acetylcholine receptor. Nature 504, 101-106 (2013).
    • (2013) Nature , vol.504 , pp. 101-106
    • Kruse, A.C.1
  • 3
    • 85016140324 scopus 로고    scopus 로고
    • Structure of CC chemokine receptor 2 with orthosteric and allosteric antagonists
    • Zheng, Y. et al. Structure of CC chemokine receptor 2 with orthosteric and allosteric antagonists. Nature 540, 458-461 (2016).
    • (2016) Nature , vol.540 , pp. 458-461
    • Zheng, Y.1
  • 4
    • 85016143647 scopus 로고    scopus 로고
    • Intracellular allosteric antagonism of the CCR9 receptor
    • Oswald, C. et al. Intracellular allosteric antagonism of the CCR9 receptor. Nature 540, 462-465 (2016).
    • (2016) Nature , vol.540 , pp. 462-465
    • Oswald, C.1
  • 5
    • 84968796800 scopus 로고    scopus 로고
    • Extra-helical binding site of a glucagon receptor antagonist
    • Jazayeri, A. et al. Extra-helical binding site of a glucagon receptor antagonist. Nature 533, 274-277 (2016).
    • (2016) Nature , vol.533 , pp. 274-277
    • Jazayeri, A.1
  • 6
    • 36448978229 scopus 로고    scopus 로고
    • 2-adrenergic receptor function
    • 2-adrenergic receptor function. Science 318, 1266-1273 (2007).
    • (2007) Science , vol.318 , pp. 1266-1273
    • Rosenbaum, D.M.1
  • 7
    • 80051658642 scopus 로고    scopus 로고
    • s protein complex
    • s protein complex. Nature 477, 549-555 (2011).
    • (2011) Nature , vol.477 , pp. 549-555
    • Rasmussen, S.G.1
  • 8
    • 84938359988 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser
    • Kang, Y. et al. Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser. Nature 523, 561-567 (2015).
    • (2015) Nature , vol.523 , pp. 561-567
    • Kang, Y.1
  • 9
    • 84978080610 scopus 로고    scopus 로고
    • Allosteric nanobodies reveal the dynamic range and diverse mechanisms of G-protein-coupled receptor activation
    • Staus, D. P. et al. Allosteric nanobodies reveal the dynamic range and diverse mechanisms of G-protein-coupled receptor activation. Nature 535, 448-452 (2016).
    • (2016) Nature , vol.535 , pp. 448-452
    • Staus, D.P.1
  • 10
    • 84886947656 scopus 로고    scopus 로고
    • 2-adrenoceptor stabilized by an engineered nanobody
    • 2-adrenoceptor stabilized by an engineered nanobody. Nature 502, 575-579 (2013).
    • (2013) Nature , vol.502 , pp. 575-579
    • Ring, A.M.1
  • 11
    • 78651411166 scopus 로고    scopus 로고
    • 2 adrenoceptor
    • 2 adrenoceptor. Nature 469, 175-180 (2011).
    • (2011) Nature , vol.469 , pp. 175-180
    • Rasmussen, S.G.1
  • 12
    • 84939795137 scopus 로고    scopus 로고
    • Structural insights into μ-opioid receptor activation
    • Huang, W. et al. Structural insights into μ-opioid receptor activation. Nature 524, 315-321 (2015).
    • (2015) Nature , vol.524 , pp. 315-321
    • Huang, W.1
  • 13
    • 0028809411 scopus 로고
    • Amino and carboxyl terminal modifcations to facilitate the production and purifcation of a G protein-coupled receptor
    • Kobilka, B. K. Amino and carboxyl terminal modifcations to facilitate the production and purifcation of a G protein-coupled receptor. Anal. Biochem. 231, 269-271 (1995).
    • (1995) Anal. Biochem. , vol.231 , pp. 269-271
    • Kobilka, B.K.1
  • 14
    • 67649392795 scopus 로고    scopus 로고
    • Crystallizing membrane proteins using lipidic mesophases
    • Cafrey, M. & Cherezov, V. Crystallizing membrane proteins using lipidic mesophases. Nat. Protoc. 4, 706-731 (2009).
    • (2009) Nat. Protoc. , vol.4 , pp. 706-731
    • Cafrey, M.1    Cherezov, V.2
  • 16
    • 33744459472 scopus 로고    scopus 로고
    • Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis
    • 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. 103, 8060-8065 (2006).
    • (2006) Proc. Natl Acad. Sci. , vol.103 , pp. 8060-8065
    • Strong, M.1
  • 17
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 19
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D 66, 12-21 (2010).
    • (2010) Acta Crystallogr. D , vol.66 , pp. 12-21
    • Chen, V.B.1
  • 20
    • 0022307515 scopus 로고
    • Fast Fourier transform calculation of electron density maps
    • Ten Eyck, L F. Fast Fourier transform calculation of electron density maps. Methods Enzymol. 115, 324-337 (1985).
    • (1985) Methods Enzymol. , vol.115 , pp. 324-337
    • Ten Eyck, L.F.1
  • 21
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Winn, M. D. et al. Overview of the CCP4 suite and current developments. Acta Crystallogr. D 67, 235-242 (2011).
    • (2011) Acta Crystallogr. D , vol.67 , pp. 235-242
    • Winn, M.D.1
  • 22
    • 84979854797 scopus 로고    scopus 로고
    • Stock-based detection of protein oligomeric states in jsPISA
    • Krissinel, E. Stock-based detection of protein oligomeric states in jsPISA. Nucleic Acids Res. 43 (W1), W314-W319 (2015).
    • (2015) Nucleic Acids Res. , vol.43 , Issue.W1 , pp. W314-W319
    • Krissinel, E.1
  • 23
    • 34250666273 scopus 로고    scopus 로고
    • A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efciently activates its G protein
    • Whorton, M. R. et al. A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efciently activates its G protein. Proc. Natl Acad. Sci. 104, 7682-7687 (2007).
    • (2007) Proc. Natl Acad. Sci. , vol.104 , pp. 7682-7687
    • Whorton, M.R.1
  • 24
    • 84900516697 scopus 로고    scopus 로고
    • Divergent transducer-specifc molecular efcacies generate biased agonism at a G protein-coupled receptor (GPCR)
    • Strachan, R. T. et al. Divergent transducer-specifc molecular efcacies generate biased agonism at a G protein-coupled receptor (GPCR). J. Biol. Chem. 289, 14211-14224 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 14211-14224
    • Strachan, R.T.1
  • 25
    • 0034603147 scopus 로고    scopus 로고
    • The efect of pH on P2 adrenoceptor function. Evidence for protonation-dependent activation
    • Ghanouni, P. et al. The efect of pH on P2 adrenoceptor function. Evidence for protonation-dependent activation. J. Biol. Chem. 275, 3121-3127 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 3121-3127
    • Ghanouni, P.1
  • 26
    • 84913603703 scopus 로고    scopus 로고
    • 250 in 32 adrenergic receptor activation from molecular dynamics simulations
    • 250 in 32 adrenergic receptor activation from molecular dynamics simulations. Biochemistry 53, 7283-7296 (2014).
    • (2014) Biochemistry , vol.53 , pp. 7283-7296
    • Ranganathan, A.1    Dror, R.O.2    Carlsson, J.3
  • 28
    • 84882643757 scopus 로고    scopus 로고
    • CHARMM36 all-atom additive protein force feld: Validation based on comparison to NMR data
    • Huang, J. & MacKerell, A. D., Jr. CHARMM36 all-atom additive protein force feld: validation based on comparison to NMR data. J. Comput Chem. 34, 2135-2145 (2013).
    • (2013) J. Comput Chem. , vol.34 , pp. 2135-2145
    • Huang, J.1    MacKerell, A.D.2
  • 29
    • 77953377650 scopus 로고    scopus 로고
    • Update of the CHARMM all-atom additive force feld for lipids: Validation on six lipid types
    • Klauda, J. B. et al. Update of the CHARMM all-atom additive force feld for lipids: validation on six lipid types. J. Phys. Chem. B 114, 7830-7843 (2010).
    • (2010) J. Phys. Chem. B , vol.114 , pp. 7830-7843
    • Klauda, J.B.1
  • 30
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • MacKerell, A. D. et al. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B 102, 3586-3616 (1998).
    • (1998) J. Phys. Chem. B , vol.102 , pp. 3586-3616
    • MacKerell, A.D.1
  • 31
    • 84865723813 scopus 로고    scopus 로고
    • 1 and X2 dihedral angles
    • 1 and X2 dihedral angles. J. Chem. Theory Comput. 8, 32573273 (2012).
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 32573273
    • Best, R.B.1
  • 32
    • 84865758046 scopus 로고    scopus 로고
    • Inclusion of many-body efects in the additive CHARMM protein CMAP potential results in enhanced cooperativity of a-helix and p-hairpin formation
    • Best, R. B., Mittal, J., Feig, M. & MacKerell, A. D., Jr. Inclusion of many-body efects in the additive CHARMM protein CMAP potential results in enhanced cooperativity of a-helix and p-hairpin formation. Biophys. J. 103, 1045-1051 (2012).
    • (2012) Biophys. J. , vol.103 , pp. 1045-1051
    • Best, R.B.1    Mittal, J.2    Feig, M.3    MacKerell, A.D.4
  • 33
    • 76249087938 scopus 로고    scopus 로고
    • CHARMM general force feld: A force feld for drug-like molecules compatible with the CHARMM all-atom additive biologica force felds
    • Vanommeslaeghe, K. et al. CHARMM general force feld: a force feld for drug-like molecules compatible with the CHARMM all-atom additive biologica force felds. J. Comput. Chem. 31, 671-690 (2010).
    • (2010) J. Comput. Chem. , vol.31 , pp. 671-690
    • Vanommeslaeghe, K.1
  • 34
    • 84871544678 scopus 로고    scopus 로고
    • Automation of the CHARMM General Force Field (CGenFF) II: Assignment of bonded parameters and partial atomic charges
    • Vanommeslaeghe, K, Raman, E. P. & MacKerell, A. D., Jr. Automation of the CHARMM General Force Field (CGenFF) II: assignment of bonded parameters and partial atomic charges. J. Chem. Inf. Model. 52, 3155-3168 (2012).
    • (2012) J. Chem. Inf. Model. , vol.52 , pp. 3155-3168
    • Vanommeslaeghe, K.1    Raman, E.P.2    MacKerell, A.D.3
  • 35
    • 84871545594 scopus 로고    scopus 로고
    • Automation of the CHARMM General Force Field (CGenFF) I: Bond perception and atom typing
    • Vanommeslaeghe, K. & MacKerell, A. D., Jr. Automation of the CHARMM General Force Field (CGenFF) I: bond perception and atom typing. J. Chem. Inf. Model. 52, 3144-3154 (2012).
    • (2012) J. Chem. Inf. Model. , vol.52 , pp. 3144-3154
    • Vanommeslaeghe, K.1    MacKerell, A.D.2
  • 36
    • 84884192184 scopus 로고    scopus 로고
    • Routine microsecond molecular dynamics simulations with AMBER on GPUs. 2. Explicit solvent particle mesh ewald
    • Salomon-Ferrer, R., Götz, A. W., Poole, D., Le Grand, S. & Walker, R. C. Routine microsecond molecular dynamics simulations with AMBER on GPUs. 2. Explicit solvent particle mesh ewald. J. Chem. Theory Comput 9, 3878-3888 (2013).
    • (2013) J. Chem. Theory Comput , vol.9 , pp. 3878-3888
    • Salomon-Ferrer, R.1    Götz, A.W.2    Poole, D.3    Le Grand, S.4    Walker, R.C.5
  • 38
    • 84927779536 scopus 로고    scopus 로고
    • Long-time-step molecular dynamics through hydrogen mass repartitioning
    • Hopkins, C. W., Le Grand, S., Walker, R. C. & Roitberg, A. E. Long-time-step molecular dynamics through hydrogen mass repartitioning. J. Chem. Theory Comput. 11, 1864-1874 (2015).
    • (2015) J. Chem. Theory Comput. , vol.11 , pp. 1864-1874
    • Hopkins, C.W.1    Le Grand, S.2    Walker, R.C.3    Roitberg, A.E.4
  • 40
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace, A. C, Laskowski, R. A. & Thornton, J. M. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8, 127-134 (1995).
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.