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Volumn 369, Issue 4, 2007, Pages 895-901

Galanthamine and Non-competitive Inhibitor Binding to ACh-binding Protein: Evidence for a Binding Site on Non-α-subunit Interfaces of Heteromeric Neuronal Nicotinic Receptors

Author keywords

acetylcholine binding protein; cocaine; galanthamine; nicotinic receptors; non competitive inhibitors

Indexed keywords

ACETYLCHOLINE; BINDING PROTEIN; COCAINE; CYSTEINE; GALANTAMINE; NICOTINIC RECEPTOR;

EID: 34248598024     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.03.067     Document Type: Article
Times cited : (105)

References (38)
  • 4
    • 0022758905 scopus 로고
    • The reaction site of a non-competitive antagonist in the delta-subunit of the nicotinic acetylcholine receptor
    • Oberthur W., Muhn P., Baumann H., Lottspeich F., Wittmann-Liebold B., and Hucho F. The reaction site of a non-competitive antagonist in the delta-subunit of the nicotinic acetylcholine receptor. EMBO J. 5 (1986) 1815-1819
    • (1986) EMBO J. , vol.5 , pp. 1815-1819
    • Oberthur, W.1    Muhn, P.2    Baumann, H.3    Lottspeich, F.4    Wittmann-Liebold, B.5    Hucho, F.6
  • 6
    • 30744470883 scopus 로고    scopus 로고
    • Probing ion-channel pores one proton at a time
    • Cymes G.D., Ni Y., and Grosman C. Probing ion-channel pores one proton at a time. Nature 438 (2005) 975-980
    • (2005) Nature , vol.438 , pp. 975-980
    • Cymes, G.D.1    Ni, Y.2    Grosman, C.3
  • 7
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • Miyazawa A., Fujiyoshi Y., and Unwin N. Structure and gating mechanism of the acetylcholine receptor pore. Nature 423 (2003) 949-955
    • (2003) Nature , vol.423 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 8
    • 0026485739 scopus 로고
    • Acetylcholine receptor channel structure probed in cysteine-substitution mutants
    • Akabas M.H., Stauffer D.A., Xu M., and Karlin A. Acetylcholine receptor channel structure probed in cysteine-substitution mutants. Science 258 (1992) 307-310
    • (1992) Science , vol.258 , pp. 307-310
    • Akabas, M.H.1    Stauffer, D.A.2    Xu, M.3    Karlin, A.4
  • 9
    • 0033046008 scopus 로고    scopus 로고
    • The steroid promegestone is a noncompetitive antagonist of the Torpedo nicotinic acetylcholine receptor that interacts with the lipid-protein interface
    • Blanton M.P., Xie Y., Dangott L.J., and Cohen J.B. The steroid promegestone is a noncompetitive antagonist of the Torpedo nicotinic acetylcholine receptor that interacts with the lipid-protein interface. Mol. Pharmacol. 55 (1999) 269-278
    • (1999) Mol. Pharmacol. , vol.55 , pp. 269-278
    • Blanton, M.P.1    Xie, Y.2    Dangott, L.J.3    Cohen, J.B.4
  • 10
    • 0142090758 scopus 로고    scopus 로고
    • Molecular mechanisms of inhibition of nicotinic acetylcholine receptors by tricyclic antidepressants
    • Gumilar F., Arias H.R., Spitzmaul G., and Bouzat C. Molecular mechanisms of inhibition of nicotinic acetylcholine receptors by tricyclic antidepressants. Neuropharmacology 45 (2003) 964-976
    • (2003) Neuropharmacology , vol.45 , pp. 964-976
    • Gumilar, F.1    Arias, H.R.2    Spitzmaul, G.3    Bouzat, C.4
  • 11
    • 0344441288 scopus 로고    scopus 로고
    • A structural model of agonist binding to the alpha3beta4 neuronal nicotinic receptor
    • Costa V., Nistri A., Cavalli A., and Carloni P. A structural model of agonist binding to the alpha3beta4 neuronal nicotinic receptor. Br. J. Pharmacol. 140 (2003) 921-931
    • (2003) Br. J. Pharmacol. , vol.140 , pp. 921-931
    • Costa, V.1    Nistri, A.2    Cavalli, A.3    Carloni, P.4
  • 12
    • 0033922960 scopus 로고    scopus 로고
    • Subtype-selective inhibition of neuronal nicotinic acetylcholine receptors by cocaine is determined by the alpha4 and beta4 subunits
    • Francis M.M., Vazquez R.W., Papke R.L., and Oswald R.E. Subtype-selective inhibition of neuronal nicotinic acetylcholine receptors by cocaine is determined by the alpha4 and beta4 subunits. Mol. Pharmacol. 58 (2000) 109-119
    • (2000) Mol. Pharmacol. , vol.58 , pp. 109-119
    • Francis, M.M.1    Vazquez, R.W.2    Papke, R.L.3    Oswald, R.E.4
  • 13
    • 33646177253 scopus 로고    scopus 로고
    • Molecular mechanisms and binding site locations for noncompetitive antagonists of nicotinic acetylcholine receptors
    • Arias H.R., Bhumireddy P., and Bouzat C. Molecular mechanisms and binding site locations for noncompetitive antagonists of nicotinic acetylcholine receptors. Int. J. Biochem. Cell Biol. 38 (2006) 1254-1276
    • (2006) Int. J. Biochem. Cell Biol. , vol.38 , pp. 1254-1276
    • Arias, H.R.1    Bhumireddy, P.2    Bouzat, C.3
  • 14
    • 23944472732 scopus 로고    scopus 로고
    • Nicotinic agonists, antagonists, and modulators from natural sources
    • Daly J.W. Nicotinic agonists, antagonists, and modulators from natural sources. Cell Mol. Neurobiol. 25 (2005) 513-552
    • (2005) Cell Mol. Neurobiol. , vol.25 , pp. 513-552
    • Daly, J.W.1
  • 15
    • 0035902187 scopus 로고    scopus 로고
    • A glia-derived acetylcholine-binding protein that modulates synaptic transmission
    • Smit A.B., Syed N.I., Schaap D., van Minnen J., Klumperman J., Kits K.S., et al. A glia-derived acetylcholine-binding protein that modulates synaptic transmission. Nature 411 (2001) 261-268
    • (2001) Nature , vol.411 , pp. 261-268
    • Smit, A.B.1    Syed, N.I.2    Schaap, D.3    van Minnen, J.4    Klumperman, J.5    Kits, K.S.6
  • 16
    • 2642560397 scopus 로고    scopus 로고
    • Structural and ligand recognition characteristics of an acetylcholine-binding protein from Aplysia californica
    • Hansen S.B., Talley T.T., Radic Z., and Taylor P. Structural and ligand recognition characteristics of an acetylcholine-binding protein from Aplysia californica. J. Biol. Chem. 279 (2004) 24197-24202
    • (2004) J. Biol. Chem. , vol.279 , pp. 24197-24202
    • Hansen, S.B.1    Talley, T.T.2    Radic, Z.3    Taylor, P.4
  • 17
    • 4344616080 scopus 로고    scopus 로고
    • Coupling of agonist binding to channel gating in an ACh-binding protein linked to an ion channel
    • Bouzat C., Gumilar F., Spitzmaul G., Wang H.L., Rayes D., Hansen S.B., et al. Coupling of agonist binding to channel gating in an ACh-binding protein linked to an ion channel. Nature 430 (2004) 896-900
    • (2004) Nature , vol.430 , pp. 896-900
    • Bouzat, C.1    Gumilar, F.2    Spitzmaul, G.3    Wang, H.L.4    Rayes, D.5    Hansen, S.B.6
  • 18
    • 14844300820 scopus 로고    scopus 로고
    • Agonist-mediated conformational changes in acetylcholine-binding protein revealed by simulation and intrinsic tryptophan fluorescence
    • Gao F., Bren N., Burghardt T.P., Hansen S., Henchman R.H., Taylor P., et al. Agonist-mediated conformational changes in acetylcholine-binding protein revealed by simulation and intrinsic tryptophan fluorescence. J. Biol. Chem. 280 (2005) 8443-8451
    • (2005) J. Biol. Chem. , vol.280 , pp. 8443-8451
    • Gao, F.1    Bren, N.2    Burghardt, T.P.3    Hansen, S.4    Henchman, R.H.5    Taylor, P.6
  • 19
    • 1842475289 scopus 로고    scopus 로고
    • Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures
    • Celie P.H., van Rossum-Fikkert S.E., van Dijk W.J., Brejc K., Smit A.B., and Sixma T.K. Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures. Neuron 41 (2004) 907-914
    • (2004) Neuron , vol.41 , pp. 907-914
    • Celie, P.H.1    van Rossum-Fikkert, S.E.2    van Dijk, W.J.3    Brejc, K.4    Smit, A.B.5    Sixma, T.K.6
  • 20
    • 0038771238 scopus 로고    scopus 로고
    • Comparative modeling of GABA(A) receptors: limits, insights, future developments
    • Ernst M., Brauchart D., Boresch S., and Sieghart W. Comparative modeling of GABA(A) receptors: limits, insights, future developments. Neuroscience 119 (2003) 933-943
    • (2003) Neuroscience , vol.119 , pp. 933-943
    • Ernst, M.1    Brauchart, D.2    Boresch, S.3    Sieghart, W.4
  • 21
    • 33748939932 scopus 로고    scopus 로고
    • Solution NMR of acetylcholine binding protein reveals agonist-mediated conformational change of the C-loop
    • Gao F., Mer G., Tonelli M., Hansen S.B., Burghardt T.P., Taylor P., and Sine S.M. Solution NMR of acetylcholine binding protein reveals agonist-mediated conformational change of the C-loop. Mol. Pharmacol. 70 (2006) 1230-1235
    • (2006) Mol. Pharmacol. , vol.70 , pp. 1230-1235
    • Gao, F.1    Mer, G.2    Tonelli, M.3    Hansen, S.B.4    Burghardt, T.P.5    Taylor, P.6    Sine, S.M.7
  • 22
    • 10744232323 scopus 로고    scopus 로고
    • Galantamine is an allosterically potentiating ligand of neuronal nicotinic but not of muscarinic acetylcholine receptors
    • Samochocki M., Hoffle A., Fehrenbacher A., Jostock R., Ludwig J., Christner C., et al. Galantamine is an allosterically potentiating ligand of neuronal nicotinic but not of muscarinic acetylcholine receptors. J. Pharmacol. Exp. Ther. 305 (2003) 1024-1036
    • (2003) J. Pharmacol. Exp. Ther. , vol.305 , pp. 1024-1036
    • Samochocki, M.1    Hoffle, A.2    Fehrenbacher, A.3    Jostock, R.4    Ludwig, J.5    Christner, C.6
  • 23
    • 33645095976 scopus 로고    scopus 로고
    • Identification of amino acid residues important for assembly of GABA receptor alpha1 and gamma2 subunits
    • Sarto-Jackson I., Ramerstorfer J., Ernst M., and Sieghart W. Identification of amino acid residues important for assembly of GABA receptor alpha1 and gamma2 subunits. J. Neurochem. 96 (2006) 983-995
    • (2006) J. Neurochem. , vol.96 , pp. 983-995
    • Sarto-Jackson, I.1    Ramerstorfer, J.2    Ernst, M.3    Sieghart, W.4
  • 24
    • 0033616681 scopus 로고    scopus 로고
    • Modulation of nicotinic acetylcholine receptors by strychnine
    • Garcia-Colunga J., and Miledi R. Modulation of nicotinic acetylcholine receptors by strychnine. Proc. Natl Acad. Sci. USA 96 (1999) 4113-4118
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 4113-4118
    • Garcia-Colunga, J.1    Miledi, R.2
  • 25
    • 0031888644 scopus 로고    scopus 로고
    • Strychnine: a potent competitive antagonist of alpha-bungarotoxin-sensitive nicotinic acetylcholine receptors in rat hippocampal neurons
    • Matsubayashi H., Alkondon M., Pereira E.F., Swanson K.L., and Albuquerque E.X. Strychnine: a potent competitive antagonist of alpha-bungarotoxin-sensitive nicotinic acetylcholine receptors in rat hippocampal neurons. J. Pharmacol. Exp. Ther. 284 (1998) 904-913
    • (1998) J. Pharmacol. Exp. Ther. , vol.284 , pp. 904-913
    • Matsubayashi, H.1    Alkondon, M.2    Pereira, E.F.3    Swanson, K.L.4    Albuquerque, E.X.5
  • 27
    • 0025808153 scopus 로고
    • A second pathway of activation of the Torpedo acetylcholine receptor channel
    • Okonjo K.O., Kuhlmann J., and Maelicke A. A second pathway of activation of the Torpedo acetylcholine receptor channel. Eur. J. Biochem. 200 (1991) 671-677
    • (1991) Eur. J. Biochem. , vol.200 , pp. 671-677
    • Okonjo, K.O.1    Kuhlmann, J.2    Maelicke, A.3
  • 28
    • 27144473613 scopus 로고    scopus 로고
    • Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations
    • Hansen S.B., Sulzenbacher G., Huxford T., Marchot P., Taylor P., and Bourne Y. Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations. EMBO J. 24 (2005) 3635-3646
    • (2005) EMBO J. , vol.24 , pp. 3635-3646
    • Hansen, S.B.1    Sulzenbacher, G.2    Huxford, T.3    Marchot, P.4    Taylor, P.5    Bourne, Y.6
  • 29
    • 0019182078 scopus 로고
    • The relationship between agonist occupation and the permeability response of the cholinergic receptor revealed by bound cobra alpha-toxin
    • Sine S.M., and Taylor P. The relationship between agonist occupation and the permeability response of the cholinergic receptor revealed by bound cobra alpha-toxin. J. Biol. Chem. 255 (1980) 10144-10156
    • (1980) J. Biol. Chem. , vol.255 , pp. 10144-10156
    • Sine, S.M.1    Taylor, P.2
  • 30
    • 0033136270 scopus 로고    scopus 로고
    • lynx1, an endogenous toxin-like modulator of nicotinic acetylcholine receptors in the mammalian CNS
    • Miwa J.M., Ibanez-Tallon I., Crabtree G.W., Sanchez R., Sali A., Role L.W., and Heintz N. lynx1, an endogenous toxin-like modulator of nicotinic acetylcholine receptors in the mammalian CNS. Neuron 23 (1999) 105-114
    • (1999) Neuron , vol.23 , pp. 105-114
    • Miwa, J.M.1    Ibanez-Tallon, I.2    Crabtree, G.W.3    Sanchez, R.4    Sali, A.5    Role, L.W.6    Heintz, N.7
  • 31
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • Reeves P.J., Callewaert N., Contreras R., and Khorana H.G. Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proc. Natl Acad. Sci. USA 99 (2002) 13419-13424
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 32
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 33
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computing Project Number 4
    • Collaborative Computing Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D 50 (1994) 760-763
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 760-763
  • 34
    • 84920325457 scopus 로고
    • AMoRe: an automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A 50 (1994) 157-163
    • (1994) Acta Crystallog. sect. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 35
    • 0002705842 scopus 로고
    • A visual protein crystallographic software system for X11/XView
    • McRee D. A visual protein crystallographic software system for X11/XView. J. Mol. Graph. 10 (1992) 44-46
    • (1992) J. Mol. Graph. , vol.10 , pp. 44-46
    • McRee, D.1
  • 36
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by maximum-likelihood method. Acta Crystallog. sect. D 53 (1997) 240-255
    • (1997) Acta Crystallog. sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 37
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4A resolution
    • Unwin N. Refined structure of the nicotinic acetylcholine receptor at 4A resolution. J. Mol. Biol. 346 (2005) 967-989
    • (2005) J. Mol. Biol. , vol.346 , pp. 967-989
    • Unwin, N.1
  • 38
    • 0035902009 scopus 로고    scopus 로고
    • Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors
    • Brejc K., van Dijk W.J., Klaassen R.V., Schuurmans M., van Der Oost J., Smit A.B., and Sixma T.K. Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors. Nature 411 (2001) 269-276
    • (2001) Nature , vol.411 , pp. 269-276
    • Brejc, K.1    van Dijk, W.J.2    Klaassen, R.V.3    Schuurmans, M.4    van Der Oost, J.5    Smit, A.B.6    Sixma, T.K.7


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