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Volumn 485, Issue 7398, 2012, Pages 327-332

Structure of the human κ-opioid receptor in complex with JDTic

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; KAPPA OPIATE RECEPTOR; KAPPA OPIATE RECEPTOR ANTAGONIST; NALTRINDOLE; NORBINALTORPHIMINE; SALVINORIN A;

EID: 84862777742     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature10939     Document Type: Article
Times cited : (769)

References (50)
  • 1
    • 0038024615 scopus 로고    scopus 로고
    • The G-proteincoupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints
    • Fredriksson, R., Lagerstrom, M. C., Lundin, L. G. & Schioth, H. B. The G-proteincoupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. Mol. Pharmacol. 63, 1256-1272 (2003).
    • (2003) Mol. Pharmacol. , vol.63 , pp. 1256-1272
    • Fredriksson, R.1    Lagerstrom, M.C.2    Lundin, L.G.3    Schioth, H.B.4
  • 3
    • 36448995359 scopus 로고    scopus 로고
    • High-resolution crystal structure of an engineered human b2-adrenergic G protein-coupled receptor
    • Cherezov, V. et al. High-resolution crystal structure of an engineered human b2-adrenergic G protein-coupled receptor. Science 318, 1258-1265 (2007).
    • (2007) Science , vol.318 , pp. 1258-1265
    • Cherezov, V.1
  • 4
    • 56749103466 scopus 로고    scopus 로고
    • The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist
    • Jaakola, V. P. et al. The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist. Science 322, 1211-1217 (2008).
    • (2008) Science , vol.322 , pp. 1211-1217
    • Jaakola, V.P.1
  • 5
    • 78449305788 scopus 로고    scopus 로고
    • Structure of the human dopamine D3 receptor in complex with a D2/D3 selective antagonist
    • Chien, E. Y. et al. Structure of the human dopamine D3 receptor in complex with a D2/D3 selective antagonist. Science 330, 1091-1095 (2010).
    • (2010) Science , vol.330 , pp. 1091-1095
    • Chien, E.Y.1
  • 6
    • 47949129742 scopus 로고    scopus 로고
    • Structure of a b1-adrenergic G-protein-coupled receptor
    • Warne, T. et al. Structure of a b1-adrenergic G-protein-coupled receptor. Nature 454, 486-491 (2008).
    • (2008) Nature , vol.454 , pp. 486-491
    • Warne, T.1
  • 7
    • 79960070651 scopus 로고    scopus 로고
    • Structure of the human histamine H1 receptor complex with doxepin
    • Shimamura, T. et al. Structure of the human histamine H1 receptor complex with doxepin. Nature 475, 65-70 (2011).
    • (2011) Nature , vol.475 , pp. 65-70
    • Shimamura, T.1
  • 8
    • 85027927015 scopus 로고    scopus 로고
    • Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists
    • Wu, B. et al. Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists. Science 330, 1066-1071 (2010).
    • (2010) Science , vol.330 , pp. 1066-1071
    • Wu, B.1
  • 9
    • 80051658642 scopus 로고    scopus 로고
    • Crystal structure of the b2 adrenergic receptor-Gs protein complex
    • Rasmussen, S. G. et al. Crystal structure of the b2 adrenergic receptor-Gs protein complex. Nature 477, 549-555 (2011).
    • (2011) Nature , vol.477 , pp. 549-555
    • Rasmussen, S.G.1
  • 10
    • 84855799592 scopus 로고    scopus 로고
    • Diversity and modularity of G proteincoupled receptor structures
    • Katritch, V., Cherezov, V. & Stevens, R. C. Diversity and modularity of G proteincoupled receptor structures. Trends Pharmacol. Sci. 33, 17-27 (2011).
    • (2011) Trends Pharmacol. Sci. , vol.33 , pp. 17-27
    • Katritch, V.1    Cherezov, V.2    Stevens, R.C.3
  • 11
    • 79960176452 scopus 로고    scopus 로고
    • Progress in structure based drug design for G protein-coupled receptors
    • Congreve, M., Langmead, C. J., Mason, J. S. & Marshall, F. H. Progress in structure based drug design for G protein-coupled receptors. J. Med. Chem. 54, 4283-4311 (2011).
    • (2011) J. Med. Chem. , vol.54 , pp. 4283-4311
    • Congreve, M.1    Langmead, C.J.2    Mason, J.S.3    Marshall, F.H.4
  • 12
    • 80051521545 scopus 로고    scopus 로고
    • Status of GPCR modeling and docking as reflected by community-wide GPCR Dock 2010 assessment
    • Kufareva, I., Rueda, M., Katritch, V., Stevens, R. C. & Abagyan, R. Status of GPCR modeling and docking as reflected by community-wide GPCR Dock 2010 assessment. Structure 19, 1108-1126 (2011).
    • (2011) Structure , vol.19 , pp. 1108-1126
    • Kufareva, I.1    Rueda, M.2    Katritch, V.3    Stevens, R.C.4    Abagyan, R.5
  • 13
    • 0017064976 scopus 로고
    • The effects of morphine-and nalorphine-like drugs in the nondependent and morphinedependent chronic spinal dog
    • Martin, W. R., Eades, C. G., Thompson, J. A., Huppler, R. E. & Gilbert, P. E. The effects of morphine-and nalorphine-like drugs in the nondependent and morphinedependent chronic spinal dog. J. Pharmacol. Exp. Ther. 197, 517-532 (1976).
    • (1976) J. Pharmacol. Exp. Ther. , vol.197 , pp. 517-532
    • Martin, W.R.1    Eades, C.G.2    Thompson, J.A.3    Huppler, R.E.4    Gilbert, P.E.5
  • 14
    • 67849088529 scopus 로고    scopus 로고
    • Kappa-opioid ligands in the study and treatment of mood disorders
    • Carlezon, W. A. Jr, Beguin, C., Knoll, A. T.&Cohen, B. M. Kappa-opioid ligands in the study and treatment of mood disorders. Pharmacol. Ther. 123, 334-343 (2009).
    • (2009) Pharmacol. Ther. , vol.123 , pp. 334-343
    • Carlezon Jr., W.A.1    Beguin, C.2    Knoll, A.T.3    Cohen, B.M.4
  • 15
    • 0037015067 scopus 로고    scopus 로고
    • Salvinorin A: A potent naturally occurring nonnitrogenous k opioid selective agonist
    • Roth, B. L. et al. Salvinorin A: a potent naturally occurring nonnitrogenous k opioid selective agonist. Proc. Natl Acad. Sci. USA 99, 11934-11939 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 11934-11939
    • Roth, B.L.1
  • 16
    • 0034873586 scopus 로고    scopus 로고
    • Enadoline a selective kappa opioid agonist: Comparison with butorphanol and hydromorphone in humans
    • Walsh, S. L., Strain, E. C., Abreu, M. E. & Bigelow, G. E. Enadoline, a selective kappa opioid agonist: comparison with butorphanol and hydromorphone in humans. Psychopharmacology (Berl.) 157, 151-162 (2001).
    • (2001) Psychopharmacology (Berl.) , vol.157 , pp. 151-162
    • Walsh, S.L.1    Strain, E.C.2    Abreu, M.E.3    Bigelow, G.E.4
  • 17
    • 0035899186 scopus 로고    scopus 로고
    • Identification of the first trans-(3R,4R)-dimethyl-4-(3-hydroxyphenyl) piperidine derivative to possess highly potent and selective opioid k receptor antagonist activity
    • Thomas, J. B. et al. Identification of the first trans-(3R,4R)-dimethyl- 4-(3-hydroxyphenyl)piperidine derivative to possess highly potent and selective opioid k receptor antagonist activity. J. Med. Chem. 44, 2687-2690 (2001).
    • (2001) J. Med. Chem. , vol.44 , pp. 2687-2690
    • Thomas, J.B.1
  • 18
    • 4644244869 scopus 로고    scopus 로고
    • Pharmacological properties of JDTic: A novel k-opioid receptor antagonist
    • Carroll, F. I. et al. Pharmacological properties of JDTic: a novel k-opioid receptor antagonist. Eur. J. Pharmacol. 501, 111-119 (2004).
    • (2004) Eur. J. Pharmacol. , vol.501 , pp. 111-119
    • Carroll, F.I.1
  • 19
    • 77953290619 scopus 로고    scopus 로고
    • Effect of the selective kappaopioid receptor antagonist JDTic on nicotine antinociception, reward, and withdrawal in the mouse
    • Jackson, K. J., Carroll, F. I., Negus, S. S. & Damaj, M. I. Effect of the selective kappaopioid receptor antagonist JDTic on nicotine antinociception, reward, and withdrawal in the mouse. Psychopharmacology (Berl.) 210, 285-294 (2010).
    • (2010) Psychopharmacology (Berl.) , vol.210 , pp. 285-294
    • Jackson, K.J.1    Carroll, F.I.2    Negus, S.S.3    Damaj, M.I.4
  • 20
    • 33750836895 scopus 로고    scopus 로고
    • Crystal structure of a photoactivated deprotonated intermediate of rhodopsin
    • Salom, D. et al. Crystal structure of a photoactivated deprotonated intermediate of rhodopsin. Proc. Natl Acad. Sci. USA 103, 16123-16128 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 16123-16128
    • Salom, D.1
  • 21
    • 48749126827 scopus 로고    scopus 로고
    • Ligandsensitivity in dimeric associations of the serotonin 5HT2c receptor
    • Mancia, F., Assur, Z.,Herman, A. G., Siegel, R.&Hendrickson, W.A. Ligandsensitivity in dimeric associations of the serotonin 5HT2c receptor. EMBO Rep. 9, 363-369 (2008).
    • (2008) EMBO Rep. , vol.9 , pp. 363-369
    • Mancia, F.1    Assur, Z.2    Herman, A.G.3    Siegel, R.4    Hendrickson, W.A.5
  • 22
    • 0028143479 scopus 로고
    • Human k opiate receptor second extracellular loop elevates dynorphin's affinity for human m/k chimeras
    • Wang, J. B., Johnson, P. S., Wu, J. M., Wang, W. F. & Uhl, G. R. Human k opiate receptor second extracellular loop elevates dynorphin's affinity for human m/k chimeras. J. Biol. Chem. 269, 25966-25969 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 25966-25969
    • Wang, J.B.1    Johnson, P.S.2    Wu, J.M.3    Wang, W.F.4    Uhl, G.R.5
  • 23
    • 77957055780 scopus 로고
    • Integrated methods for the construction of threedimensional models and computational probing of structure-function relations in G protein-coupled receptors
    • Ballesteros, J. A. & Weinstein, H. Integrated methods for the construction of threedimensional models and computational probing of structure-function relations in G protein-coupled receptors. Methods Neurosci. 25, 366-428 (1995).
    • (1995) Methods Neurosci. , vol.25 , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 24
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G protein-coupled receptor
    • Palczewski, K. et al. Crystal structure of rhodopsin: a G protein-coupled receptor. Science 289, 739-745 (2000).
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1
  • 25
    • 79954782236 scopus 로고    scopus 로고
    • Structure of an agonist-bound human A2A adenosine receptor
    • Xu, F. et al. Structure of an agonist-bound human A2A adenosine receptor. Science 332, 322-327 (2011).
    • (2011) Science , vol.332 , pp. 322-327
    • Xu, F.1
  • 26
    • 79953242234 scopus 로고    scopus 로고
    • The structural basis of agonist-induced activation in constitutively active rhodopsin
    • Standfuss, J. et al. The structural basis of agonist-induced activation in constitutively active rhodopsin. Nature 471, 656-660 (2011).
    • (2011) Nature , vol.471 , pp. 656-660
    • Standfuss, J.1
  • 27
    • 7844249248 scopus 로고    scopus 로고
    • Conformational analysis and automated receptor docking of selective arylacetamide-based k-opioid agonists
    • Subramanian, G., Paterlini, M. G., Larson, D. L., Portoghese, P. S. & Ferguson, D. M. Conformational analysis and automated receptor docking of selective arylacetamide-based k-opioid agonists. J. Med. Chem. 41, 4777-4789 (1998).
    • (1998) J. Med. Chem. , vol.41 , pp. 4777-4789
    • Subramanian, G.1    Paterlini, M.G.2    Larson, D.L.3    Portoghese, P.S.4    Ferguson, D.M.5
  • 28
    • 41149171838 scopus 로고    scopus 로고
    • Synthesis and in vitro opioid receptor functional antagonism of analogues of the selective kappa opioid receptor antagonist (3R)-7-hydroxy-N-((1S)-1- {[(3R,4R)-4-(3-hydroxyphenyl)-3, 4-dimethyl-1-pipe ridinyl]methyl}-2- methylpropyl)-1,2,3,4-tetrahydro-3-isoquinolinecarboxamide (JDTic)
    • Cai, T. B. et al. Synthesis and in vitro opioid receptor functional antagonism of analogues of the selective kappa opioid receptor antagonist (3R)-7-hydroxy-N-((1S)-1-{[(3R,4R)-4-(3-hydroxyphenyl)-3,4-dimethyl-1-pipe ridinyl]methyl}-2-methylpropyl)-1,2,3,4-tetrahydro-3-isoquinolinecarboxamide (JDTic). J. Med. Chem. 51, 1849-1860 (2008).
    • (2008) J. Med. Chem , vol.51 , pp. 1849-1860
    • Cai, T.B.1
  • 29
    • 0842325908 scopus 로고    scopus 로고
    • Importance of phenolic address groups in opioid kappa receptor selective antagonists
    • Thomas, J. B. et al. Importance of phenolic address groups in opioid kappa receptor selective antagonists. J. Med. Chem. 47, 1070-1073 (2004).
    • (2004) J. Med. Chem. , vol.47 , pp. 1070-1073
    • Thomas, J.B.1
  • 30
    • 77954752369 scopus 로고    scopus 로고
    • Analogues of (3R)-7-hydroxy-N-[(1S)-1-{[(3R,4R)-4-(3-hydroxyphenyl)-3,4- dimethyl-1-pipe ridinyl]methyl}-2-methylpropyl)-1,2,3,4-tetrahydro-3- isoquinolinecarboxamide (JDTic). Synthesis and in vitro and in vivo opioid receptor antagonist activity
    • Runyon, S. P. et al. Analogues of (3R)-7-hydroxy-N-[(1S)-1-{[(3R,4R)-4- (3-hydroxyphenyl)-3,4-dimethyl-1-pipe ridinyl]methyl}-2-methylpropyl)-1,2,3,4- tetrahydro-3-isoquinolinecarboxamide (JDTic). Synthesis and in vitro and in vivo opioid receptor antagonist activity. J. Med. Chem. 53, 5290-5301 (2010).
    • (2010) J. Med. Chem , vol.53 , pp. 5290-5301
    • Runyon, S.P.1
  • 31
    • 0018135396 scopus 로고
    • New structural concepts for narcotic antagonists defined in a 4-phenylpiperidine series
    • Zimmerman, D. M., Nickander, R., Horng, J. S. & Wong, D. T. New structural concepts for narcotic antagonists defined in a 4-phenylpiperidine series. Nature 275, 332-334 (1978).
    • (1978) Nature , vol.275 , pp. 332-334
    • Zimmerman, D.M.1    Nickander, R.2    Horng, J.S.3    Wong, D.T.4
  • 32
    • 34047253035 scopus 로고    scopus 로고
    • Differential helical orientations among related G protein-coupled receptors provide a novel mechanism for selectivity. Studies with salvinorin A and the k-opioid receptor
    • Vortherms, T. A., Mosier, P. D., Westkaemper, R. B. & Roth, B. L. Differential helical orientations among related G protein-coupled receptors provide a novel mechanism for selectivity. Studies with salvinorin A and the k-opioid receptor. J. Biol. Chem. 282, 3146-3156 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 3146-3156
    • Vortherms, T.A.1    Mosier, P.D.2    Westkaemper, R.B.3    Roth, B.L.4
  • 33
    • 0028170438 scopus 로고
    • Mu opiate receptor. Charged transmembrane domain amino acids are critical for agonist recognition and intrinsic activity
    • Surratt, C. K. et al.-mu opiate receptor. Charged transmembrane domain amino acids are critical for agonist recognition and intrinsic activity. J. Biol. Chem. 269, 20548-20553 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 20548-20553
    • Surratt, C.K.1
  • 34
    • 0030040907 scopus 로고    scopus 로고
    • The conserved aspartate residue in the third putative transmembrane domain of the delta-opioid receptor is not the anionic counterpart for cationic opiate binding but is a constituent of the receptor binding site
    • Befort, K. et al. The conserved aspartate residue in the third putative transmembrane domain of the delta-opioid receptor is not the anionic counterpart for cationic opiate binding but is a constituent of the receptor binding site. Mol. Pharmacol. 49, 216-223 (1996).
    • (1996) Mol. Pharmacol. , vol.49 , pp. 216-223
    • Befort, K.1
  • 35
    • 0031302358 scopus 로고    scopus 로고
    • Flexible protein-ligand docking by global energy optimization in internal coordinates
    • Totrov, M. & Abagyan, R. Flexible protein-ligand docking by global energy optimization in internal coordinates. Proteins 29, 215-220 (1997).
    • (1997) Proteins , vol.29 , pp. 215-220
    • Totrov, M.1    Abagyan, R.2
  • 36
    • 0029994263 scopus 로고    scopus 로고
    • Application of the message-address concept to the docking of naltrexone and selective naltrexonederived opioid antagonists into opioid receptor models
    • Metzger, T. G., Paterlini, M. G., Portoghese, P. S.&Ferguson, D. M. Application of the message-address concept to the docking of naltrexone and selective naltrexonederived opioid antagonists into opioid receptor models. Neurochem. Res. 21, 1287-1294 (1996).
    • (1996) Neurochem. Res. , vol.21 , pp. 1287-1294
    • Metzger, T.G.1    Paterlini, M.G.2    Portoghese, P.S.3    Ferguson, D.M.4
  • 37
    • 0037076531 scopus 로고    scopus 로고
    • Mutation of a single TMVI residue, Phe282, in the b2-adrenergic receptor results in structurally distinct activated receptor conformations
    • Chen, S. et al. Mutation of a single TMVI residue, Phe282, in the b2-adrenergic receptor results in structurally distinct activated receptor conformations. Biochemistry 41, 6045-6053 (2002).
    • (2002) Biochemistry , vol.41 , pp. 6045-6053
    • Chen, S.1
  • 38
    • 0345158331 scopus 로고
    • Specific receptor for the opioid peptide dynorphin: Structure-activity relationships
    • Chavkin, C. & Goldstein, A. Specific receptor for the opioid peptide dynorphin: structure-activity relationships. Proc. Natl Acad. Sci. USA 78, 6543-6547 (1981).
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 6543-6547
    • Chavkin, C.1    Goldstein, A.2
  • 39
    • 67651204566 scopus 로고    scopus 로고
    • Structure-based design synthesis and biochemical and pharmacological characterization of novel salvinorin A analogues as active state probes of the k-opioid receptor
    • Yan, F. et al. Structure-based design, synthesis, and biochemical and pharmacological characterization of novel salvinorin A analogues as active state probes of the k-opioid receptor. Biochemistry 48, 6898-6908 (2009).
    • (2009) Biochemistry , vol.48 , pp. 6898-6908
    • Yan, F.1
  • 41
    • 36448978229 scopus 로고    scopus 로고
    • GPCR engineering yields high-resolution structural insights into b2-adrenergic receptor function
    • Rosenbaum, D. M. et al. GPCR engineering yields high-resolution structural insights into b2-adrenergic receptor function. Science 318, 1266-1273 (2007).
    • (2007) Science , vol.318 , pp. 1266-1273
    • Rosenbaum, D.M.1
  • 42
    • 67649392795 scopus 로고    scopus 로고
    • Crystallizing membrane proteins using lipidic mesophases
    • Caffrey, M. & Cherezov, V. Crystallizing membrane proteins using lipidic mesophases. Nature Protocols 4, 706-731 (2009).
    • (2009) Nature Protocols , vol.4 , pp. 706-731
    • Caffrey, M.1    Cherezov, V.2
  • 43
    • 9944252602 scopus 로고    scopus 로고
    • A robotic system for crystallizing membrane and soluble proteins in lipidic mesophases
    • Cherezov, V., Peddi, A., Muthusubramaniam, L., Zheng, Y. F. & Caffrey, M. A robotic system for crystallizing membrane and soluble proteins in lipidic mesophases. Acta Crystallogr. D 60, 1795-1807 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 1795-1807
    • Cherezov, V.1    Peddi, A.2    Muthusubramaniam, L.3    Zheng, Y.F.4    Caffrey, M.5
  • 44
    • 69949132434 scopus 로고    scopus 로고
    • Rastering strategy for screening and centring of microcrystal samples of human membrane proteins with a sub-10 mm size X-ray synchrotron beam
    • Cherezov, V. et al. Rastering strategy for screening and centring of microcrystal samples of human membrane proteins with a sub-10 mm size X-ray synchrotron beam. J. R. Soc. Interface 6 (Suppl. 5), S587-S597 (2009).
    • (2009) J. R. Soc. Interface , vol.6 , Issue.SUPPL. 5
    • Cherezov, V.1
  • 45
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 46
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Cryst. 40, 658-674 (2007).
    • (2007) J. Appl. Cryst. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 47
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A. & Dodson, E. J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240-255 (1997).
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 49
    • 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


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