메뉴 건너뛰기




Volumn 288, Issue 48, 2013, Pages 34470-34483

Chemotype-selective modes of action of κ-opioid receptor agonists

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION MECHANISMS; AGONIST BINDING SITE; FUNCTIONAL ASSAYS; MOLECULAR DETERMINANTS; OPIOID RECEPTORS; RECEPTOR ACTIVATION; RECEPTOR BINDING; SITE DIRECTED MUTAGENESIS;

EID: 84889011912     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.515668     Document Type: Article
Times cited : (61)

References (47)
  • 1
    • 34248596144 scopus 로고    scopus 로고
    • Cloning and bioinformatics of amphibian μ, δ, κ, and nociceptin opioid receptors expressed in brain tissue. Evidence for opioid receptor divergence in mammals
    • Stevens, C. W., Brasel, C. M., and Mohan, S. (2007) Cloning and bioinformatics of amphibian μ, δ, κ, and nociceptin opioid receptors expressed in brain tissue. Evidence for opioid receptor divergence in mammals. Neurosci. Lett. 419, 189-194
    • (2007) Neurosci. Lett , vol.419 , pp. 189-194
    • Stevens, C.W.1    Brasel, C.M.2    Mohan, S.3
  • 6
    • 84872221774 scopus 로고    scopus 로고
    • Structure-function of the G protein-coupled receptor superfamily
    • Katritch, V., Cherezov, V., and Stevens, R. C. (2013) Structure-function of the G protein-coupled receptor superfamily. Annu. Rev. Pharmacol. Toxicol. 53, 531-556
    • (2013) Annu Rev Pharmacol Toxicol , vol.53 , pp. 531-556
    • Katritch, V.1    Cherezov, V.2    Stevens, R.C.3
  • 7
    • 84855799592 scopus 로고    scopus 로고
    • Diversity and modularity ofGprotein-coupled receptor structures
    • Katritch, V., Cherezov, V., and Stevens, R. C. (2012) Diversity and modularity ofGprotein-coupled receptor structures. Trends Pharmacol. Sci. 33, 17-27
    • (2012) Trends Pharmacol Sci , vol.33 , pp. 17-27
    • Katritch, V.1    Cherezov, V.2    Stevens, R.C.3
  • 8
    • 84871286519 scopus 로고    scopus 로고
    • Restructuring G-protein-coupled receptor activation
    • Audet, M., and Bouvier, M. (2012) Restructuring G-protein-coupled receptor activation. Cell 151, 14-23
    • (2012) Cell , vol.151 , pp. 14-23
    • Audet, M.1    Bouvier, M.2
  • 9
    • 84873306058 scopus 로고    scopus 로고
    • Conformational ensembles in GPCR activation
    • Vardy, E., and Roth, B. L. (2013) Conformational ensembles in GPCR activation. Cell 152, 385-386
    • (2013) Cell , vol.152 , pp. 385-386
    • Vardy, E.1    Roth, B.L.2
  • 10
    • 84875475404 scopus 로고    scopus 로고
    • Discovery of a novel selective δ-opioid receptor agonist using crystal structure-based virtual screening
    • Negri, A., Rives, M.-L., Caspers, M. J., Prisinzano, T. E., Javitch, J. A., and Filizola, M. (2013) Discovery of a novel selective δ-opioid receptor agonist using crystal structure-based virtual screening. J. Chem. Inf. Model. 53, 521-526
    • (2013) J. Chem. Inf. Model , vol.53 , pp. 521-526
    • Negri, A.1    Rives, M.-L.2    Caspers, M.J.3    Prisinzano, T.E.4    Javitch, J.A.5    Filizola, M.6
  • 11
    • 80054795187 scopus 로고    scopus 로고
    • GPCR agonist binding revealed by modeling and crystallography
    • Katritch, V., and Abagyan, R. (2011) GPCR agonist binding revealed by modeling and crystallography. Trends Pharmacol. Sci. 32, 637-643
    • (2011) Trends Pharmacol. Sci , vol.32 , pp. 637-643
    • Katritch, V.1    Abagyan, R.2
  • 12
    • 67650239912 scopus 로고    scopus 로고
    • Analysis of full and partial agonists binding to β2-adrenergic receptor suggests a role of transmembrane helix v in agonist-specific conformational changes
    • Katritch, V., Reynolds, K. A., Cherezov, V., Hanson, M. A., Roth, C. B., Yeager, M., and Abagyan, R. (2009) Analysis of full and partial agonists binding to β2-adrenergic receptor suggests a role of transmembrane helix V in agonist-specific conformational changes. J. Mol. Recognit. 22, 307-318
    • (2009) J. Mol. Recognit , vol.22 , pp. 307-318
    • Katritch, V.1    Reynolds, K.A.2    Cherezov, V.3    Hanson, M.A.4    Roth, C.B.5    Yeager, M.6    Abagyan, R.7
  • 14
    • 0034611604 scopus 로고    scopus 로고
    • Isosteric replacement of acidic with neutral residues in extracellular loop-2 of theδ-opioid receptor does not affect dynorphin A(1-13) affinity and function
    • Ferguson, D. M., Kramer, S., Metzger, T. G., Law, P. Y., and Portoghese, P. S. (2000) Isosteric replacement of acidic with neutral residues in extracellular loop-2 of theδ-opioid receptor does not affect dynorphin A(1-13) affinity and function. J. Med. Chem. 43, 1251-1252
    • (2000) J. Med. Chem , vol.43 , pp. 1251-1252
    • Ferguson, D.M.1    Kramer, S.2    Metzger, T.G.3    Law, P.Y.4    Portoghese, P.S.5
  • 15
    • 0029959123 scopus 로고    scopus 로고
    • Radioligand-dependent discrepancy in agonist affinities enhanced by mutations in the δ-opioid receptor
    • Hjorth, S. A., Thirstrup, K., and Schwartz, T. W. (1996) Radioligand-dependent discrepancy in agonist affinities enhanced by mutations in the δ-opioid receptor. Mol. Pharmacol. 50, 977-984
    • (1996) Mol. Pharmacol , vol.50 , pp. 977-984
    • Hjorth, S.A.1    Thirstrup, K.2    Schwartz, T.W.3
  • 16
    • 41149143712 scopus 로고    scopus 로고
    • Toward a structure- based model of salvinorin A recognition of the δ-opioid receptor
    • Kane, B. E., McCurdy, C. R., and Ferguson, D. M. (2008) Toward a structure- based model of salvinorin A recognition of the δ-opioid receptor. J. Med. Chem. 51, 1824-1830
    • (2008) J. Med. Chem , vol.51 , pp. 1824-1830
    • Kane, B.E.1    McCurdy, C.R.2    Ferguson, D.M.3
  • 17
    • 0035866624 scopus 로고    scopus 로고
    • Investigation of the selectivity of oxymorphone- and naltrexonederived ligands via site-directed mutagenesis of opioid receptors. Exploring the "address" recognition locus
    • Metzger, T. G., Paterlini, M. G., Ferguson, D. M., and Portoghese, P. S. (2001) Investigation of the selectivity of oxymorphone- and naltrexonederived ligands via site-directed mutagenesis of opioid receptors. Exploring the "address" recognition locus. J. Med. Chem. 44, 857-862
    • (2001) J. Med. Chem , vol.44 , pp. 857-862
    • Metzger, T.G.1    Paterlini, M.G.2    Ferguson, D.M.3    Portoghese, P.S.4
  • 18
    • 0036176035 scopus 로고    scopus 로고
    • Determinants of ligand selectivity at the κ-receptor based on the structure of the orphanin FQ receptor
    • Owens, C. E., and Akil, H. (2002) Determinants of ligand selectivity at the κ-receptor based on the structure of the orphanin FQ receptor. J. Pharmacol. Exp. Ther. 300, 992-999
    • (2002) J. Pharmacol. Exp. Ther , vol.300 , pp. 992-999
    • Owens, C.E.1    Akil, H.2
  • 19
    • 0024405504 scopus 로고
    • Bivalent ligands and the message-address concept in the design of selective opioid receptor antagonists
    • Portoghese, P. S. (1989) Bivalent ligands and the message-address concept in the design of selective opioid receptor antagonists. Trends Pharmacol. Sci. 10, 230-235
    • (1989) Trends Pharmacol. Sci , vol.10 , pp. 230-235
    • Portoghese, P.S.1
  • 20
    • 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 δ-opioid receptor
    • Yan, F., Bikbulatov, R. V., Mocanu, V., Dicheva, N., Parker, C. E., Wetsel, W. C., Mosier, P. D., Westkaemper, R. B., Allen, J. A., Zjawiony, J. K., and Roth, B. L. (2009) Structure-based design, synthesis, and biochemical and pharmacological characterization of novel salvinorin A analogues as active state probes of the δ-opioid receptor. Biochemistry 48, 6898-6908
    • (2009) Biochemistry , vol.48 , pp. 6898-6908
    • Yan, F.1    Bikbulatov, R.V.2    Mocanu, V.3    Dicheva, N.4    Parker, C.E.5    Wetsel, W.C.6    Mosier, P.D.7    Westkaemper, R.B.8    Allen, J.A.9    Zjawiony, J.K.10    Roth, B.L.11
  • 22
    • 0345158331 scopus 로고
    • Specific receptor for the opioid peptide dynorphin. Structure-activity relationships
    • Chavkin, C., and Goldstein, A. (1981) Specific receptor for the opioid peptide dynorphin. Structure-activity relationships. Proc. Natl. Acad. Sci. U.S.A. 78, 6543-6547
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 6543-6547
    • Chavkin, C.1    Goldstein, A.2
  • 23
    • 71049131594 scopus 로고    scopus 로고
    • The effects of C-terminal modifications on the opioid activity of [N-benzylTyr1]dynorphin A-(1-11) analogues
    • Patkar, K. A., Murray, T. F., and Aldrich, J. V. (2009) The effects of C-terminal modifications on the opioid activity of [N-benzylTyr1]dynorphin A-(1-11) analogues. J. Med. Chem. 52, 6814-6821
    • (2009) J. Med. Chem , vol.52 , pp. 6814-6821
    • Patkar, K.A.1    Murray, T.F.2    Aldrich, J.V.3
  • 25
    • 77956162799 scopus 로고    scopus 로고
    • N-Alkyl-octahydroisoquinolin-1-one-8-carboxamides. Selective and nonbasicδ-opioid receptor ligands
    • Frankowski, K. J., Ghosh, P., Setola, V., Tran, T. B., Roth, B. L., and Aubé, J. (2010) N-Alkyl-octahydroisoquinolin-1-one-8-carboxamides. Selective and nonbasicδ-opioid receptor ligands. ACS Med. Chem. Lett. 1, 189-193
    • (2010) ACS Med. Chem. Lett , vol.1 , pp. 189-193
    • Frankowski, K.J.1    Ghosh, P.2    Setola, V.3    Tran, T.B.4    Roth, B.L.5    Aubé, J.6
  • 28
    • 84863823908 scopus 로고    scopus 로고
    • How opioid drugs bind to receptors
    • Filizola, M., and Devi, L. A. (2012) How opioid drugs bind to receptors. Nature 485, 314-317
    • (2012) Nature , vol.485 , pp. 314-317
    • Filizola, M.1    Devi, L.A.2
  • 29
    • 0032123424 scopus 로고    scopus 로고
    • Structure-activity relationship studies of dynorphin A and related peptides
    • Naqvi, T., Haq, W., and Mathur, K. B. (1998) Structure-activity relationship studies of dynorphin A and related peptides. Peptides 19, 1277-1292
    • (1998) Peptides , vol.19 , pp. 1277-1292
    • Naqvi, T.1    Haq, W.2    Mathur, K.B.3
  • 30
    • 0028099965 scopus 로고
    • Amino acids in the cloned mouse receptor that are necessary for high affinity agonist binding but not antagonist binding
    • Kong, H., Raynor, K., and Reisine, T. (1994) Amino acids in the cloned mouse receptor that are necessary for high affinity agonist binding but not antagonist binding. Regul. Pept. 54, 155-156
    • (1994) Regul. Pept , vol.54 , pp. 155-156
    • Kong, H.1    Raynor, K.2    Reisine, T.3
  • 31
    • 0028143479 scopus 로고
    • Human κ opiate receptor second extracellular loop elevates dynorphin's affinity for human μ/κ chimeras
    • Wang, J. B., Johnson, P. S., Wu, J. M., Wang, W. F., and Uhl, G. R. (1994) Human κ opiate receptor second extracellular loop elevates dynorphin's affinity for human μ/κ chimeras. J. Biol. Chem. 269, 25966 -25969
    • (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
  • 32
    • 0028882923 scopus 로고
    • The cloned μ, δ and κ receptors and their endogenous ligands. Evidence for two opioid peptide recognition cores
    • Mansour, A., Hoversten, M. T., Taylor, L. P., Watson, S. J., and Akil, H. (1995) The cloned μ, δ and κ receptors and their endogenous ligands. Evidence for two opioid peptide recognition cores. Brain Res. 700, 89 -98
    • (1995) Brain Res , vol.700 , pp. 89-98
    • Mansour, A.1    Hoversten, M.T.2    Taylor, L.P.3    Watson, S.J.4    Akil, H.5
  • 33
    • 0034692171 scopus 로고    scopus 로고
    • Binding of norbinaltorphimine (nor-BNI) congeners to wild type and mutant μ and κ opioid receptors. Molecular recognition loci for the pharmacophore and address components of κ antagonists
    • Larson, D. L., Jones, R. M., Hjorth, S. A., Schwartz, T. W., and Portoghese, P. S. (2000) Binding of norbinaltorphimine (nor-BNI) congeners to wild type and mutant μ and κ opioid receptors. Molecular recognition loci for the pharmacophore and address components of κ antagonists. J. Med. Chem. 43, 1573-1576
    • (2000) J. Med. Chem , vol.43 , pp. 1573-1576
    • Larson, D.L.1    Jones, R.M.2    Hjorth, S.A.3    Schwartz, T.W.4    Portoghese, P.S.5
  • 34
    • 0035927440 scopus 로고    scopus 로고
    • Transformation of a δ-opioid receptor antagonist to a κ-agonist by transfer of a guanidinium group from the 5'- to 6'-position of naltrindole
    • Sharma, S. K., Jones, R. M., Metzger, T. G., Ferguson, D. M., and Portoghese, P. S. (2001) Transformation of a δ-opioid receptor antagonist to a κ-agonist by transfer of a guanidinium group from the 5'- to 6'-position of naltrindole. J. Med. Chem. 44, 2073-2079
    • (2001) J. Med. Chem , vol.44 , pp. 2073-2079
    • Sharma, S.K.1    Jones, R.M.2    Metzger, T.G.3    Ferguson, D.M.4    Portoghese, P.S.5
  • 35
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig, B., and Nicholls, A. (1995) Classical electrostatics in biology and chemistry. Science 268, 1144-1149
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 36
    • 0032570306 scopus 로고    scopus 로고
    • A cluster of aromatic residues in the sixth membrane-spanning segment of the dopamine D2 receptor is accessible in the binding-site crevice
    • Javitch, J. A., Ballesteros, J. A., Weinstein, H., and Chen, J. (1998) A cluster of aromatic residues in the sixth membrane-spanning segment of the dopamine D2 receptor is accessible in the binding-site crevice. Biochemistry 37, 998-1006
    • (1998) Biochemistry , vol.37 , pp. 998-1006
    • Javitch, J.A.1    Ballesteros, J.A.2    Weinstein, H.3    Chen, J.4
  • 38
    • 0034119969 scopus 로고    scopus 로고
    • A highly conserved aspartic acid (Asp 155) anchors the terminal amine moiety of tryptamines and is involved in membrane targeting of the 5-HT2A serotonin receptor but does not participate in activation via a "salt-bridge disruption" mechanism
    • Kristiansen, K., Kroeze, W. K., Willins, D. L., Gelber, E. I., and Savage, J. E. (2000) A highly conserved aspartic acid (Asp 155) anchors the terminal amine moiety of tryptamines and is involved in membrane targeting of the 5-HT2A serotonin receptor but does not participate in activation via a "salt-bridge disruption" mechanism. J. Pharmacol. Exp. Ther. 293, 735-746
    • (2000) J. Pharmacol. Exp. Ther , vol.293 , pp. 735-746
    • Kristiansen, K.1    Kroeze, W.K.2    Willins, D.L.3    Gelber, E.I.4    Savage, J.E.5
  • 39
    • 0028022026 scopus 로고
    • Site-directed mutagenesis of the histamine H1 receptor. Roles of aspartic acid107, asparagine198 and threonine194
    • Ohta, K., Hayashi, H., Mizuguchi, H., Kagamiyama, H., Fujimoto, K., and Fukui, H. (1994) Site-directed mutagenesis of the histamine H1 receptor. Roles of aspartic acid107, asparagine198 and threonine194. Biochem. Biophys. Res. Commun. 203, 1096-1101
    • (1994) Biochem. Biophys. Res. Commun , vol.203 , pp. 1096-1101
    • Ohta, K.1    Hayashi, H.2    Mizuguchi, H.3    Kagamiyama, H.4    Fujimoto, K.5    Fukui, H.6
  • 40
    • 0023740863 scopus 로고
    • Conserved aspartic acid residues 79 and 113 of the β-adrenergic receptor have different roles in receptor function
    • Strader, C. D., Sigal, I. S., Candelore, M. R., Rands, E., Hill, W. S., and Dixon, R. A. (1988) Conserved aspartic acid residues 79 and 113 of the β-adrenergic receptor have different roles in receptor function. J. Biol. Chem. 263, 10267-10271
    • (1988) J. Biol. Chem , vol.263 , pp. 10267-10271
    • Strader, C.D.1    Sigal, I.S.2    Candelore, M.R.3    Rands, E.4    Hill, W.S.5    Dixon, R.A.6
  • 46
    • 84862776738 scopus 로고    scopus 로고
    • Biased signaling pathways in β2-adrenergic receptor characterized by 19FNMR
    • Liu, J. J., Horst, R., Katritch, V., Stevens, R. C., and Wüthrich, K. (2012) Biased signaling pathways in β2-adrenergic receptor characterized by 19FNMR. Science 335, 1106-1110
    • (2012) Science , vol.335 , pp. 1106-1110
    • Liu, J.J.1    Horst, R.2    Katritch, V.3    Stevens, R.C.4    Wüthrich, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.