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Volumn 22, Issue 9, 2003, Pages 1990-2003

An H-bond between two residues from different loops of the acetylcholine binding site contributes to the activation mechanism of nicotinic receptors

Author keywords

bungarotoxin binding; Activation mechanism; H bond; Myasthenic mutant; Neuronal nicotinic receptor

Indexed keywords

ACETYLCHOLINE; ALPHA BUNGAROTOXIN; AMINO ACID; BINDING PROTEIN; CHIMERIC PROTEIN; CHOLINERGIC RECEPTOR; EPIBATIDINE; NICOTINE; NICOTINIC RECEPTOR; SEROTONIN 3 RECEPTOR;

EID: 0037544107     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdg197     Document Type: Article
Times cited : (54)

References (38)
  • 2
    • 0021504608 scopus 로고
    • The use of double mutants to detect structural changes in the active site of the tyrosyMRNA synthetase (Bacillus stearothermophilus)
    • Carter, P.J., Winter, G., Wilkinson, A.J. and Fersht, A.R. (1984) The use of double mutants to detect structural changes in the active site of the tyrosyMRNA synthetase (Bacillus stearothermophilus). Cell, 38, 835-840.
    • (1984) Cell , vol.38 , pp. 835-840
    • Carter, P.J.1    Winter, G.2    Wilkinson, A.J.3    Fersht, A.R.4
  • 3
    • 0004195760 scopus 로고    scopus 로고
    • University of California, San Francisco, CA
    • Case, D.A. et al. (2002) AMBER 7. University of California, San Francisco, CA.
    • (2002) AMBER 7
    • Case, D.A.1
  • 5
    • 0029078817 scopus 로고
    • Identification of a new component of the agonist binding site of the nicotinic α7 homooligomeric receptor
    • Corringer, P.J., Galzi, J.-L., Eisele, J.-L., Bertrand, S., Changeux, J.-P. and Bertrand, D. (1995) Identification of a new component of the agonist binding site of the nicotinic α7 homooligomeric receptor. J. Biol. Chem., 270, 11749-11752.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11749-11752
    • Corringer, P.J.1    Galzi, J.-L.2    Eisele, J.-L.3    Bertrand, S.4    Changeux, J.-P.5    Bertrand, D.6
  • 6
    • 0031972835 scopus 로고    scopus 로고
    • Critical elements determining diversity in agonist binding and desensitization of neuronal nicotinic acetylcholine receptors
    • Corringer, P.J., Bertrand, S., Bohler, S., Edelstein, S.J., Changeux, J.-P. and Bertrand, D. (1998) Critical elements determining diversity in agonist binding and desensitization of neuronal nicotinic acetylcholine receptors. J. Neurosci., 18, 648-657.
    • (1998) J. Neurosci. , vol.18 , pp. 648-657
    • Corringer, P.J.1    Bertrand, S.2    Bohler, S.3    Edelstein, S.J.4    Changeux, J.-P.5    Bertrand, D.6
  • 8
    • 0030987817 scopus 로고    scopus 로고
    • Mutations in different functional domains of the human muscle acetylcholine receptor α subunit in patients with the slow-channel congenital myasthenic syndrome
    • Croxen, R., Newland, C., Beeson, D., Oosterhuis, H., Chauplannaz, G., Vincent, A. and Newsom-Davis, J. (1997) Mutations in different functional domains of the human muscle acetylcholine receptor α subunit in patients with the slow-channel congenital myasthenic syndrome. Hum. Mol. Genet., 6, 767-774.
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 767-774
    • Croxen, R.1    Newland, C.2    Beeson, D.3    Oosterhuis, H.4    Chauplannaz, G.5    Vincent, A.6    Newsom-Davis, J.7
  • 9
    • 0030281174 scopus 로고    scopus 로고
    • A kinetic mechanism for nicotinic acetylcholine receptors based on multiple allosteric transitions
    • Edelstein, S.J., Schaad, O., Henry, E., Bertrand, D. and Changeux, J.-P. (1996) A kinetic mechanism for nicotinic acetylcholine receptors based on multiple allosteric transitions. Biol. Cybern., 75, 361-379.
    • (1996) Biol. Cybern. , vol.75 , pp. 361-379
    • Edelstein, S.J.1    Schaad, O.2    Henry, E.3    Bertrand, D.4    Changeux, J.-P.5
  • 10
    • 0027772476 scopus 로고
    • Chimaeric nicotinic-serotonergic receptor combines distinct ligand binding and channel specificities
    • Eiselé, J.-L., Bertrand, S., Galzi, J.-L., Devillers-Thiéry, A., Changeux, J.-P. and Bertrand, D. (1993) Chimaeric nicotinic-serotonergic receptor combines distinct ligand binding and channel specificities. Nature, 366, 479-483.
    • (1993) Nature , vol.366 , pp. 479-483
    • Eiselé, J.-L.1    Bertrand, S.2    Galzi, J.-L.3    Devillers-Thiéry, A.4    Changeux, J.-P.5    Bertrand, D.6
  • 12
    • 0025753149 scopus 로고
    • Allosteric transitions of the acetylcholine receptor probed at the amino acid level with a photolabile cholinergic ligand
    • Galzi, J.-L., Revah, F., Bouet, F., Menez, A., Goeldner, M., Hirth, C. and Changeux, J.-P. (1991) Allosteric transitions of the acetylcholine receptor probed at the amino acid level with a photolabile cholinergic ligand. Proc. Natl Acad. Sci. USA, 88, 5051-5055.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5051-5055
    • Galzi, J.-L.1    Revah, F.2    Bouet, F.3    Menez, A.4    Goeldner, M.5    Hirth, C.6    Changeux, J.-P.7
  • 14
    • 0033811476 scopus 로고    scopus 로고
    • The extracellular linker of muscle acetylcholine receptor channels is a gating control element
    • Grosman, C., Salamone, F.N., Sine, S.M. and Auerbach, A. (2000) The extracellular linker of muscle acetylcholine receptor channels is a gating control element. J. Gen. Physiol., 116, 327-340.
    • (2000) J. Gen. Physiol. , vol.116 , pp. 327-340
    • Grosman, C.1    Salamone, F.N.2    Sine, S.M.3    Auerbach, A.4
  • 15
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N. and Peitsch, M.C. (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis, 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 16
    • 0019441262 scopus 로고
    • Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches
    • Hamill, O.P., Marty, A., Neher, E., Sakmann, B. and Sigworth, F.J. (1981) Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches. Pflugers Arch., 391, 85-100.
    • (1981) Pflugers Arch. , vol.391 , pp. 85-100
    • Hamill, O.P.1    Marty, A.2    Neher, E.3    Sakmann, B.4    Sigworth, F.J.5
  • 17
  • 18
    • 17944368301 scopus 로고    scopus 로고
    • The binding site of acetylcholine receptor as visualized in the X-ray structure of a complex between α-bungarotoxin and a mimotope peptide
    • Harel, M. et al. (2001) The binding site of acetylcholine receptor as visualized in the X-ray structure of a complex between α-bungarotoxin and a mimotope peptide. Neuron, 32, 265-275.
    • (2001) Neuron , vol.32 , pp. 265-275
    • Harel, M.1
  • 20
    • 0028981913 scopus 로고
    • α-conotoxin ImI exhibits subtype-specific nicotinic acetylcholine receptor blockade: Preferential inhibition of homomeric α7 and α9 receptors
    • Johnson, D.S., Martinez, J., Elgoyhen, A.B., Heinemann, S.F. and Mclntosh, J.M. (1995) α-Conotoxin ImI exhibits subtype-specific nicotinic acetylcholine receptor blockade: preferential inhibition of homomeric α7 and α9 receptors. Mol. Pharmacol., 48, 194-199.
    • (1995) Mol. Pharmacol. , vol.48 , pp. 194-199
    • Johnson, D.S.1    Martinez, J.2    Elgoyhen, A.B.3    Heinemann, S.F.4    Mclntosh, J.M.5
  • 21
    • 0036480194 scopus 로고    scopus 로고
    • Emerging structure of the nicotinic acetylcholine receptors
    • Karlin, A. (2002) Emerging structure of the nicotinic acetylcholine receptors. Nat. Rev. Neurosci., 3, 102-114.
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 102-114
    • Karlin, A.1
  • 25
    • 0030815133 scopus 로고    scopus 로고
    • RASTER3D: Photorealistic molecular graphics
    • Merritt, E.A. and Bacon, D.J. (1997) RASTER3D: photorealistic molecular graphics. Methods Enzymol., 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 26
    • 0037023750 scopus 로고    scopus 로고
    • NMR structural analysis of α-bungarotoxin and its complex with the principal α-neurotoxin-binding sequence on the α7 subunit of a neuronal nicotinic acetylcholine receptor
    • Moise, L., Piserchio, A., Basus, V.J. and Hawrot, E. (2002) NMR structural analysis of α-bungarotoxin and its complex with the principal α-neurotoxin-binding sequence on the α7 subunit of a neuronal nicotinic acetylcholine receptor. J. Biol. Chem., 277, 12406-12417.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12406-12417
    • Moise, L.1    Piserchio, A.2    Basus, V.J.3    Hawrot, E.4
  • 27
    • 0037172669 scopus 로고    scopus 로고
    • Residues in the ε subunit of the nicotinic acetylcholine receptor interact to confer selectivity of Waglerin-1 for the α-ε subunit interface site
    • Molles, B.E., Tsigelny, I., Nguyen, P.D., Gao, S.X., Sine, S.M. and Taylor, P. (2002) Residues in the ε subunit of the nicotinic acetylcholine receptor interact to confer selectivity of Waglerin-1 for the α-ε subunit interface site. Biochemistry, 41, 7895-7906.
    • (2002) Biochemistry , vol.41 , pp. 7895-7906
    • Molles, B.E.1    Tsigelny, I.2    Nguyen, P.D.3    Gao, S.X.4    Sine, S.M.5    Taylor, P.6
  • 28
    • 0033515532 scopus 로고    scopus 로고
    • Subunit interface selectivity of the α-neurotoxins for the nicotinic acetylcholine receptor
    • Osaka, H., Malany, S., Kanter, J.R., Sine, S.M. and Taylor, P. (1999) Subunit interface selectivity of the α-neurotoxins for the nicotinic acetylcholine receptor. J. Biol. Chem., 274, 9581-9586.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9581-9586
    • Osaka, H.1    Malany, S.2    Kanter, J.R.3    Sine, S.M.4    Taylor, P.5
  • 29
    • 0034090930 scopus 로고    scopus 로고
    • Pairwise electrostatic interactions between α-neurotoxins and γ, δ and ε subunits of the nicotinic acetylcholine receptor
    • Osaka, H., Malany, S., Molles, B.E., Sine, S.M. and Taylor, P. (2000) Pairwise electrostatic interactions between α-neurotoxins and γ, δ and ε subunits of the nicotinic acetylcholine receptor. J. Biol. Chem., 275, 5478-5484.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5478-5484
    • Osaka, H.1    Malany, S.2    Molles, B.E.3    Sine, S.M.4    Taylor, P.5
  • 30
    • 0029670737 scopus 로고    scopus 로고
    • Neuronal nicotinic α7 receptor expressed in Xenopus oocytes presents five putative binding sites for methyllycaconitine
    • Palma, E., Bertrand, S., Binzoni, T. and Bertrand, D. (1996) Neuronal nicotinic α7 receptor expressed in Xenopus oocytes presents five putative binding sites for methyllycaconitine. J. Physiol., 491, 151-161.
    • (1996) J. Physiol. , vol.491 , pp. 151-161
    • Palma, E.1    Bertrand, S.2    Binzoni, T.3    Bertrand, D.4
  • 31
    • 0032079457 scopus 로고    scopus 로고
    • Identification of residues in the neuronal α7 acetylcholine receptor that confer selectivity for conotoxin ImI
    • Quiram, P.A. and Sine, S.M. (1998) Identification of residues in the neuronal α7 acetylcholine receptor that confer selectivity for conotoxin ImI. J. Biol. Chem., 273, 11001-11006.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11001-11006
    • Quiram, P.A.1    Sine, S.M.2
  • 32
    • 0037130458 scopus 로고    scopus 로고
    • The mechanism for acetylcholine receptor inhibition by α-neurotoxins and species-specific resistance to α-bungarotoxin revealed by NMR
    • Samson, A., Scherf, T., Eisenstein, M., Chill, J. and Anglister, J. (2002) The mechanism for acetylcholine receptor inhibition by α-neurotoxins and species-specific resistance to α-bungarotoxin revealed by NMR. Neuron, 35, 319-332.
    • (2002) Neuron , vol.35 , pp. 319-332
    • Samson, A.1    Scherf, T.2    Eisenstein, M.3    Chill, J.4    Anglister, J.5
  • 33
    • 0001607746 scopus 로고    scopus 로고
    • Snake neurotoxins that interact with nicotinic acetylcholine receptors
    • Massaro, E.J. (ed.), Humana Press, Totowa, NJ
    • Servent, D. and Ménez, A. (2001) Snake neurotoxins that interact with nicotinic acetylcholine receptors. In Massaro, E.J. (ed.), Handbook of Neurotoxicology, Vol. 1. Humana Press, Totowa, NJ, pp. 385-425.
    • (2001) Handbook of Neurotoxicology , vol.1 , pp. 385-425
    • Servent, D.1    Ménez, A.2
  • 34
    • 0029087136 scopus 로고
    • Mutation of the acetylcholine receptor α subunit causes a slow-channel myasthenic syndrome by enhancing agonist binding affinity
    • Sine, M.S., Ohno, K., Bouzat, C., Auerbach, A., Milone, M., Pruit, J.N. and Engel, A.G. (1995) Mutation of the acetylcholine receptor α subunit causes a slow-channel myasthenic syndrome by enhancing agonist binding affinity. Neuron, 15, 229-239.
    • (1995) Neuron , vol.15 , pp. 229-239
    • Sine, M.S.1    Ohno, K.2    Bouzat, C.3    Auerbach, A.4    Milone, M.5    Pruit, J.N.6    Engel, A.G.7
  • 35
    • 0035902187 scopus 로고    scopus 로고
    • A glia-derived acetylcholine binding protein that modulates synaptic transmission
    • Smit, A.B. et al. (2001) A glia-derived acetylcholine binding protein that modulates synaptic transmission. Nature, 411, 261-268.
    • (2001) Nature , vol.411 , pp. 261-268
    • Smit, A.B.1
  • 36
    • 0037067680 scopus 로고    scopus 로고
    • How do short neurotoxins bind to a muscular-type nicotinic acetylcholine receptor?
    • Teixeira-Clerc, F., Ménez, A. and Kessler, P. (2002) How do short neurotoxins bind to a muscular-type nicotinic acetylcholine receptor? J. Biol. Chem., 277, 25741-25747.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25741-25747
    • Teixeira-Clerc, F.1    Ménez, A.2    Kessler, P.3
  • 37
    • 0036304564 scopus 로고    scopus 로고
    • Activation of the nicotinic acetylcholine receptor involves a switch in conformation of the α subunits
    • Unwin, N., Miyazawa, A., Li, J. and Fujiyoshi, Y. (2002) Activation of the nicotinic acetylcholine receptor involves a switch in conformation of the α subunits. J. Mol. Biol., 319, 1165-1176.
    • (2002) J. Mol. Biol. , vol.319 , pp. 1165-1176
    • Unwin, N.1    Miyazawa, A.2    Li, J.3    Fujiyoshi, Y.4
  • 38
    • 0032102496 scopus 로고    scopus 로고
    • The location of the gate in the acetylcholine receptor channel
    • Wilson, G.G. and Karlin, A. (1998) The location of the gate in the acetylcholine receptor channel. Neuron, 20, 1269-1281.
    • (1998) Neuron , vol.20 , pp. 1269-1281
    • Wilson, G.G.1    Karlin, A.2


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