메뉴 건너뛰기




Volumn 346, Issue 4, 2005, Pages 967-989

Refined structure of the nicotinic acetylcholine receptor at 4 Å resolution

Author keywords

Acetylcholine receptor; Electron microscopy; Ion channel; Refinement

Indexed keywords

NICOTINIC RECEPTOR; RECEPTOR SUBUNIT;

EID: 13444271681     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.12.031     Document Type: Article
Times cited : (1477)

References (76)
  • 2
    • 2542443504 scopus 로고    scopus 로고
    • Function and structure in glycine receptors and some of their relatives
    • D. Colquhoun, and L.G. Sivilotti Function and structure in glycine receptors and some of their relatives Trends Neurosci. 27 2004 337 344
    • (2004) Trends Neurosci. , vol.27 , pp. 337-344
    • Colquhoun, D.1    Sivilotti, L.G.2
  • 3
    • 1642383081 scopus 로고    scopus 로고
    • Mechanisms of channel gating of the ligand-gated ion channel superfamily inferred from protein structure
    • N.L. Absalom, T.M. Lewis, and P.R. Schofield Mechanisms of channel gating of the ligand-gated ion channel superfamily inferred from protein structure Expt. Physiol. 89 2004 145 153
    • (2004) Expt. Physiol. , vol.89 , pp. 145-153
    • Absalom, N.L.1    Lewis, T.M.2    Schofield, P.R.3
  • 5
    • 0036480194 scopus 로고    scopus 로고
    • Emerging structure of the nicotinic acetylcholine receptors
    • A. Karlin Emerging structure of the nicotinic acetylcholine receptors Nature Rev. Neurosci. 3 2002 102 114
    • (2002) Nature Rev. Neurosci. , vol.3 , pp. 102-114
    • Karlin, A.1
  • 8
    • 0036891560 scopus 로고    scopus 로고
    • The nicotinic receptor ligand binding domain
    • S.M. Sine The nicotinic receptor ligand binding domain J. Neurobiol. 53 2002 431 446
    • (2002) J. Neurobiol. , vol.53 , pp. 431-446
    • Sine, S.M.1
  • 9
    • 1842475289 scopus 로고    scopus 로고
    • Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures
    • P.H.N. Celie, S.E. van Rossum-Fikkert, J.W. van Dijk, K. Brejc, and A.B. Smit 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.N.1    Van Rossum-Fikkert, S.E.2    Van Dijk, J.W.3    Brejc, K.4    Smit, A.B.5
  • 10
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • A. Miyazawa, Y. Fujiyoshi, and N. Unwin 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
  • 11
    • 33748573642 scopus 로고    scopus 로고
    • The influence of geometry, surface character, and flexibility on the permeation of ions and water through biological pores
    • O. Beckstein, and M.S.P. Sansom The influence of geometry, surface character, and flexibility on the permeation of ions and water through biological pores Phys. Biol. 1 2004 42 52
    • (2004) Phys. Biol. , vol.1 , pp. 42-52
    • Beckstein, O.1    Sansom, M.S.P.2
  • 12
    • 2442548865 scopus 로고    scopus 로고
    • Theoretical conformation of the closed and open states of the acetylcholine receptor channel
    • B. Corry Theoretical conformation of the closed and open states of the acetylcholine receptor channel Biochim. Biophys. Acta 1663 2004 2 5
    • (2004) Biochim. Biophys. Acta , vol.1663 , pp. 2-5
    • Corry, B.1
  • 13
    • 0027506299 scopus 로고
    • Nicotinic acetylcholine receptor at 9 Å resolution
    • N. Unwin Nicotinic acetylcholine receptor at 9 Å resolution J. Mol. Biol. 229 1993 1101 1124
    • (1993) J. Mol. Biol. , vol.229 , pp. 1101-1124
    • Unwin, N.1
  • 14
    • 0032967642 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor at 4.6 Å resolution: Transverse tunnels in the channel wall
    • A. Miyazawa, Y. Fujiyoshi, M. Stowell, and N. Unwin Nicotinic acetylcholine receptor at 4.6 Å resolution: transverse tunnels in the channel wall J. Mol. Biol. 288 1999 765 786
    • (1999) J. Mol. Biol. , vol.288 , pp. 765-786
    • Miyazawa, A.1    Fujiyoshi, Y.2    Stowell, M.3    Unwin, N.4
  • 15
    • 0021723207 scopus 로고
    • Tubular crystals of acetylcholine receptor
    • A. Brisson, and P.N.T. Unwin Tubular crystals of acetylcholine receptor J. Cell Biol. 99 1984 1202 1211
    • (1984) J. Cell Biol. , vol.99 , pp. 1202-1211
    • Brisson, A.1    Unwin, P.N.T.2
  • 16
    • 0025678678 scopus 로고
    • Three-dimensional structure of the acetylcholine receptor by cryoelectron microscopy and helical image reconstruction
    • C. Toyoshima, and N. Unwin Three-dimensional structure of the acetylcholine receptor by cryoelectron microscopy and helical image reconstruction J. Cell Biol. 111 1990 2623 2635
    • (1990) J. Cell Biol. , vol.111 , pp. 2623-2635
    • Toyoshima, C.1    Unwin, N.2
  • 17
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • N. Unwin Acetylcholine receptor channel imaged in the open state Nature 373 1995 37 43
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 18
    • 0036304564 scopus 로고    scopus 로고
    • Activation of the nicotinic acetylcholine receptor involves a switch in conformation of the α subunits
    • N. Unwin, A. Miyazawa, J. Li, and Y. Fujiyoshi Activation of the nicotinic acetylcholine receptor involves a switch in conformation of the α subunits J. Mol. Biol. 319 2002 1165 1176
    • (2002) J. Mol. Biol. , vol.319 , pp. 1165-1176
    • Unwin, N.1    Miyazawa, A.2    Li, J.3    Fujiyoshi, Y.4
  • 20
    • 0022458822 scopus 로고
    • The ion channel of the nicotinic acetylcholine receptor is formed by the homologous helices MII of the receptor subunits
    • F.L. Hucho, W. Oberthur, and F. Lottspeich The ion channel of the nicotinic acetylcholine receptor is formed by the homologous helices MII of the receptor subunits FEBS Letters 205 1986 137 142
    • (1986) FEBS Letters , vol.205 , pp. 137-142
    • Hucho, F.L.1    Oberthur, W.2    Lottspeich, F.3
  • 21
    • 0023748825 scopus 로고
    • Rings of negatively charged amino acids determine the acetylcholine receptor channel conductance
    • K. Imoto, C. Busch, B. Sakmann, M. Mishina, T. Konno, and J. Nakai Rings of negatively charged amino acids determine the acetylcholine receptor channel conductance Nature 335 1988 645 648
    • (1988) Nature , vol.335 , pp. 645-648
    • Imoto, K.1    Busch, C.2    Sakmann, B.3    Mishina, M.4    Konno, T.5    Nakai, J.6
  • 22
    • 0026082583 scopus 로고
    • Location of a threonine residue in the α-subunit M2 transmembrane segment that determines the ion flow through the acetylcholine receptor channel
    • A. Villarroel, S. Herlitze, M. Koenen, and B. Sakmann Location of a threonine residue in the α-subunit M2 transmembrane segment that determines the ion flow through the acetylcholine receptor channel Proc. Roy. Soc. ser. B 243 1991 69 74
    • (1991) Proc. Roy. Soc. Ser. B , vol.243 , pp. 69-74
    • Villarroel, A.1    Herlitze, S.2    Koenen, M.3    Sakmann, B.4
  • 23
    • 0026625673 scopus 로고
    • Agonist-induced changes in the structure of the acetylcholine receptor M2 regions revealed by photoincorporation of an uncharged nicotinic noncompetitive antagonist
    • B.H. White, and J.B. Cohen Agonist-induced changes in the structure of the acetylcholine receptor M2 regions revealed by photoincorporation of an uncharged nicotinic noncompetitive antagonist J. Biol. Chem. 267 1992 15770 15783
    • (1992) J. Biol. Chem. , vol.267 , pp. 15770-15783
    • White, B.H.1    Cohen, J.B.2
  • 24
    • 0027987062 scopus 로고
    • Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the α subunit
    • M.H. Akabas, C. Kaufmann, P. Archdeacon, and A. Karlin Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the α subunit Neuron 13 1994 919 927
    • (1994) Neuron , vol.13 , pp. 919-927
    • Akabas, M.H.1    Kaufmann, C.2    Archdeacon, P.3    Karlin, A.4
  • 25
    • 0029085766 scopus 로고
    • Molecular dissection of subunit interfaces in the acetylcholine receptor: Identification of determinants of α-conotoxin M1 selectivity
    • S.M. Sine, H.-J. Kreienkamp, N. Bren, R. Maeda, and P. Taylor Molecular dissection of subunit interfaces in the acetylcholine receptor: identification of determinants of α-conotoxin M1 selectivity Neuron 15 1995 205 211
    • (1995) Neuron , vol.15 , pp. 205-211
    • Sine, S.M.1    Kreienkamp, H.-J.2    Bren, N.3    Maeda, R.4    Taylor, P.5
  • 26
    • 0029163027 scopus 로고
    • Channel gating governed symmetrically by conserved leucine residues in the M2 domain of nicotinic receptors
    • C. Labarca, M.W. Nowak, H. Zhang, L. Tang, P. Deshpande, and H.A. Lester Channel gating governed symmetrically by conserved leucine residues in the M2 domain of nicotinic receptors Nature 376 1995 514 516
    • (1995) Nature , vol.376 , pp. 514-516
    • Labarca, C.1    Nowak, M.W.2    Zhang, H.3    Tang, L.4    Deshpande, P.5    Lester, H.A.6
  • 27
    • 0032514762 scopus 로고    scopus 로고
    • From ab initio quantum mechanics to molecular neurobiology: A cation-pi binding site in the nicotinic receptor
    • W. Zhong, J.P. Gallivan, Y. Zhang, L. Li, H.A. Lester, and D.A. Dougherty From ab initio quantum mechanics to molecular neurobiology: a cation-pi binding site in the nicotinic receptor Proc. Natl Acad. Sci. USA 95 1998 12008 12093
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12008-12093
    • Zhong, W.1    Gallivan, J.P.2    Zhang, Y.3    Li, L.4    Lester, H.A.5    Dougherty, D.A.6
  • 28
    • 0033811476 scopus 로고    scopus 로고
    • The extracellular linker of muscle acetylcholine receptor channels is a gating control element
    • C. Grosman, F.N. Salamone, S.M. Sine, and A. Auerbach The extracellular linker of muscle acetylcholine receptor channels is a gating control element J. Gen. Physiol. 116 2000 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
  • 29
    • 0021930295 scopus 로고
    • Quaternary structure of the acetylcholine receptor
    • A. Brisson, and P.N.T. Unwin Quaternary structure of the acetylcholine receptor Nature 315 1985 474 477
    • (1985) Nature , vol.315 , pp. 474-477
    • Brisson, A.1    Unwin, P.N.T.2
  • 30
    • 0017729997 scopus 로고
    • Molecular forms of acetylcholine receptor. Effects of calcium ions and sulfhydryl reagent on the occurrence of oligomers
    • H.W. Chang, and E. Bock Molecular forms of acetylcholine receptor. Effects of calcium ions and sulfhydryl reagent on the occurrence of oligomers Biochemistry 16 1977 4513 4520
    • (1977) Biochemistry , vol.16 , pp. 4513-4520
    • Chang, H.W.1    Bock, E.2
  • 31
    • 0017741717 scopus 로고
    • Disulfide bond cross-linked dimer in acetylcholine receptor from Torpedo californica
    • S.L. Hamilton, M. McLaughlin, and A. Karlin Disulfide bond cross-linked dimer in acetylcholine receptor from Torpedo californica Biochem. Biophys. Res. Commun. 79 1977 692 699
    • (1977) Biochem. Biophys. Res. Commun. , vol.79 , pp. 692-699
    • Hamilton, S.L.1    McLaughlin, M.2    Karlin, A.3
  • 32
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.-Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallog. sect. A 47 1991 110 119
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 33
    • 0031460411 scopus 로고    scopus 로고
    • Distortion correction of tubular crystals: Improvements in the acetylcholine receptor structure
    • R. Beroukhim, and N. Unwin Distortion correction of tubular crystals: improvements in the acetylcholine receptor structure Ultramicroscopy 70 1997 57 81
    • (1997) Ultramicroscopy , vol.70 , pp. 57-81
    • Beroukhim, R.1    Unwin, N.2
  • 34
    • 0010214174 scopus 로고
    • Amphipathic analysis and possible formation of the ion channel in an acetylcholine receptor
    • J. Finer-Moore, and R.M. Stroud Amphipathic analysis and possible formation of the ion channel in an acetylcholine receptor Proc. Natl Acad. Sci. USA 81 1984 155 159
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 155-159
    • Finer-Moore, J.1    Stroud, R.M.2
  • 35
    • 85021531015 scopus 로고
    • Chemical modification of the active site of the acetylcholine receptor
    • A. Karlin Chemical modification of the active site of the acetylcholine receptor J. Gen. Physiol. 54 1969 245s 264s
    • (1969) J. Gen. Physiol. , vol.54
    • Karlin, A.1
  • 36
    • 0037047296 scopus 로고    scopus 로고
    • Lysine scanning mutagenesis delineates structural model of the nicotinic acetylcholine receptor ligand binding domain
    • S.M. Sine, H.L. Wang, and N. Bren Lysine scanning mutagenesis delineates structural model of the nicotinic acetylcholine receptor ligand binding domain J. Biol. Chem. 277 2002 29210 29223
    • (2002) J. Biol. Chem. , vol.277 , pp. 29210-29223
    • Sine, S.M.1    Wang, H.L.2    Bren, N.3
  • 37
    • 0029143458 scopus 로고
    • Three-dimensional location of the main immunogenic region of the acetylcholine receptor
    • R. Beroukhim, and N. Unwin Three-dimensional location of the main immunogenic region of the acetylcholine receptor Neuron 15 1995 323 331
    • (1995) Neuron , vol.15 , pp. 323-331
    • Beroukhim, R.1    Unwin, N.2
  • 38
    • 0034065330 scopus 로고    scopus 로고
    • Acetylcholine receptors and myasthenia
    • J.M. Lindstrom Acetylcholine receptors and myasthenia Muscle Nerve 23 2000 453 477
    • (2000) Muscle Nerve , vol.23 , pp. 453-477
    • Lindstrom, J.M.1
  • 39
    • 17344372846 scopus 로고    scopus 로고
    • Anatomy of the antigenic structure of a large membrane autoantigen, the muscle-type nicotinic acetylcholine receptor
    • S.J. Tzartos, T. Barkas, M.T. Cung, A. Mamalaki, P. Orlewski, and D. Papanastasiou Anatomy of the antigenic structure of a large membrane autoantigen, the muscle-type nicotinic acetylcholine receptor Immunol. Rev. 163 1998 89 120
    • (1998) Immunol. Rev. , vol.163 , pp. 89-120
    • Tzartos, S.J.1    Barkas, T.2    Cung, M.T.3    Mamalaki, A.4    Orlewski, P.5    Papanastasiou, D.6
  • 40
    • 0027287799 scopus 로고
    • Amino acid residues within the sequence region alpha 55-74 of Torpedo acetylcholine receptor interacting with antibodies to the main immunogenic region and with snake alpha-neurotoxins
    • J.L. Wahlsten, J.M. Lindstrom, and B.M. Cont-Tronconi Amino acid residues within the sequence region alpha 55-74 of Torpedo acetylcholine receptor interacting with antibodies to the main immunogenic region and with snake alpha-neurotoxins J. Recept. Res. 13 1993 989 1008
    • (1993) J. Recept. Res. , vol.13 , pp. 989-1008
    • Wahlsten, J.L.1    Lindstrom, J.M.2    Cont-Tronconi, B.M.3
  • 41
    • 0030424262 scopus 로고    scopus 로고
    • Compared structures of the free nicotinic acetylcholine receptor main immunogenic region (MIR) decapeptide and the antibody-bound [A76]MIR analogue: A molecular dynamics simulation from two-dimensional NMR data
    • P. Orlewski, M. Marraud, M.T. Cung, V. Tsikaris, M. Sakarellos- Daitsiotis, and C. Sakarellos Compared structures of the free nicotinic acetylcholine receptor main immunogenic region (MIR) decapeptide and the antibody-bound [A76]MIR analogue: a molecular dynamics simulation from two-dimensional NMR data Biopolymers 40 1996 419 432
    • (1996) Biopolymers , vol.40 , pp. 419-432
    • Orlewski, P.1    Marraud, M.2    Cung, M.T.3    Tsikaris, V.4    Sakarellos-Daitsiotis, M.5    Sakarellos, C.6
  • 42
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • J. Monod, J. Wyman, and J.-P. Changeux On the nature of allosteric transitions: a plausible model J. Mol. Biol. 12 1965 88 118
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 44
    • 0020047892 scopus 로고
    • A newly recognised congenital myasthenic syndrome attributed to a prolonged open time of the acetylcholine-induced ion channel
    • A.G. Engel, E.H. Lambert, D.M. Mulder, C.F. Torres, K. Sahashi, T.E. Bertorini, and J.N. Whitaker A newly recognised congenital myasthenic syndrome attributed to a prolonged open time of the acetylcholine-induced ion channel Ann. Neurol. 11 1982 553 569
    • (1982) Ann. Neurol. , vol.11 , pp. 553-569
    • Engel, A.G.1    Lambert, E.H.2    Mulder, D.M.3    Torres, C.F.4    Sahashi, K.5    Bertorini, T.E.6    Whitaker, J.N.7
  • 45
    • 0029087136 scopus 로고
    • Mutation of the acetylcholine receptor alpha subunit causes a slow-channel myasthenic syndrome by enhancing agonist binding affinity
    • S.M. Sine, K. Ohno, A. Bouzat, A. Auerbach, M. Milone, J.N. Pruitt, and A.G. Engel Mutation of the acetylcholine receptor alpha subunit causes a slow-channel myasthenic syndrome by enhancing agonist binding affinity Neuron 15 1995 229 239
    • (1995) Neuron , vol.15 , pp. 229-239
    • Sine, S.M.1    Ohno, K.2    Bouzat, A.3    Auerbach, A.4    Milone, M.5    Pruitt, J.N.6    Engel, A.G.7
  • 46
    • 0026758178 scopus 로고
    • Mutational analysis of ligand-induced activation of the Torpedo acetylcholine receptor
    • M.E. O'Leary, and M.M. White Mutational analysis of ligand-induced activation of the Torpedo acetylcholine receptor J. Biol. Chem. 267 1992 8360 8365
    • (1992) J. Biol. Chem. , vol.267 , pp. 8360-8365
    • O'Leary, M.E.1    White, M.M.2
  • 47
    • 0029859799 scopus 로고    scopus 로고
    • Binding sites contribute unequally to the gating of mouse nicotinic D200N acetylcholine receptors
    • G. Akk, S. Sine, and A. Auerbach Binding sites contribute unequally to the gating of mouse nicotinic D200N acetylcholine receptors J. Physiol. (London) 496 1996 185 196
    • (1996) J. Physiol. (London) , vol.496 , pp. 185-196
    • Akk, G.1    Sine, S.2    Auerbach, A.3
  • 48
    • 0029934560 scopus 로고    scopus 로고
    • Voltage dependence of mouse acetylcholine receptor gating: Different charge movements in di-, mono- and unliganded receptors
    • A. Auerbach, W. Sigurdson, J. Chen, and G. Akk Voltage dependence of mouse acetylcholine receptor gating: different charge movements in di-, mono- and unliganded receptors J. Physiol. (London) 494 1996 155 170
    • (1996) J. Physiol. (London) , vol.494 , pp. 155-170
    • Auerbach, A.1    Sigurdson, W.2    Chen, J.3    Akk, G.4
  • 49
    • 0035884572 scopus 로고    scopus 로고
    • Aromatics at the murine nicotinic receptor agonist binding site: Mutational analysis of the αy93 and αw149 residues
    • G. Akk Aromatics at the murine nicotinic receptor agonist binding site: mutational analysis of the αY93 and αW149 residues J. Physiol. (London) 535 2001 729 740
    • (2001) J. Physiol. (London) , vol.535 , pp. 729-740
    • Akk, G.1
  • 50
    • 0029153305 scopus 로고
    • Activation kinetics of recombinant mouse nicotinic acetylcholine receptors: Mutations of α-subunit tyrosine 190 affect both binding and gating
    • J. Chen, Y. Zhang, G. Akk, S. Sine, and A. Auerbach Activation kinetics of recombinant mouse nicotinic acetylcholine receptors: mutations of α-subunit tyrosine 190 affect both binding and gating Biophys. J. 69 1995 849 859
    • (1995) Biophys. J. , vol.69 , pp. 849-859
    • Chen, J.1    Zhang, Y.2    Akk, G.3    Sine, S.4    Auerbach, A.5
  • 51
    • 0032938313 scopus 로고    scopus 로고
    • A mutational analysis of the acetylcholine receptor channel transmitter binding site
    • G. Akk, M. Zhou, and A. Auerbach A mutational analysis of the acetylcholine receptor channel transmitter binding site Biophys. J. 76 1999 207 218
    • (1999) Biophys. J. , vol.76 , pp. 207-218
    • Akk, G.1    Zhou, M.2    Auerbach, A.3
  • 53
    • 0347379903 scopus 로고    scopus 로고
    • Role of charged residues in coupling ligand binding and channel activation in the extracellular domain of the glycine receptor
    • N.L. Absalom, T.M. Lewis, W. Kaplan, K.D. Pierce, and P.R. Schofield Role of charged residues in coupling ligand binding and channel activation in the extracellular domain of the glycine receptor J. Biol. Chem. 278 2003 50151 50157
    • (2003) J. Biol. Chem. , vol.278 , pp. 50151-50157
    • Absalom, N.L.1    Lewis, T.M.2    Kaplan, W.3    Pierce, K.D.4    Schofield, P.R.5
  • 54
    • 0242268392 scopus 로고    scopus 로고
    • Conformation-dependent hydrophobic labelling of the nicotinic receptor: Electrophysiology-coordinated photochemistry and mass spectrometry
    • J.F. Leite, M.P. Blanton, M. Shahgholi, D.A. Dougherty, and H.A. Lester Conformation-dependent hydrophobic labelling of the nicotinic receptor: electrophysiology-coordinated photochemistry and mass spectrometry Proc. Natl Acad. Sci. USA 100 2003 13054 13059
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 13054-13059
    • Leite, J.F.1    Blanton, M.P.2    Shahgholi, M.3    Dougherty, D.A.4    Lester, H.A.5
  • 55
    • 0037969585 scopus 로고    scopus 로고
    • 191 segment is involved in GABA binding and channel gating
    • 191 segment is involved in GABA binding and channel gating J. Biol. Chem. 287 2003 13166 13172
    • (2003) J. Biol. Chem. , vol.287 , pp. 13166-13172
    • Newell, J.G.1    Czajkowski, C.2
  • 56
    • 4344616080 scopus 로고    scopus 로고
    • Structural network coupling agonist binding to channel gating revealed by ACh-binding protein linked to ion channel
    • C. Bouzat, F. Gumilar, G. Spitzmaul, H.-L. Wang, D. Rayes, and S.B. Hansen Structural network coupling agonist binding to channel gating revealed by ACh-binding protein linked to 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
  • 57
    • 0027403316 scopus 로고
    • Design, synthesis and functional characterisation of a pentameric channel protein that mimics the presumed pore structure of the nicotinic cholinergic receptor
    • M.O. Montal, T. Iwamoto, J.M. Tomich, and M. Montal Design, synthesis and functional characterisation of a pentameric channel protein that mimics the presumed pore structure of the nicotinic cholinergic receptor FEBS Letters 320 1993 261 266
    • (1993) FEBS Letters , vol.320 , pp. 261-266
    • Montal, M.O.1    Iwamoto, T.2    Tomich, J.M.3    Montal, M.4
  • 58
    • 0037044793 scopus 로고    scopus 로고
    • A receptor M2-M3 loop secondary structure and changes in accessibility during channel gating
    • A receptor M2-M3 loop secondary structure and changes in accessibility during channel gating J. Biol. Chem. 277 2002 43002 43010
    • (2002) J. Biol. Chem. , vol.277 , pp. 43002-43010
    • Bera, A.K.1    Chatav, M.2    Akabas, M.H.3
  • 59
    • 0032215090 scopus 로고    scopus 로고
    • Allosteric receptors after 30 years
    • J.P. Changeux, and S.J. Edelstein Allosteric receptors after 30 years Neuron 21 1998 959 980
    • (1998) Neuron , vol.21 , pp. 959-980
    • Changeux, J.P.1    Edelstein, S.J.2
  • 60
    • 0034677524 scopus 로고    scopus 로고
    • Mapping the conformational wave of acetylcholine receptor gating
    • C. Grosman, M. Zhou, and A. Auerbach Mapping the conformational wave of acetylcholine receptor gating Nature 403 2000 773 776
    • (2000) Nature , vol.403 , pp. 773-776
    • Grosman, C.1    Zhou, M.2    Auerbach, A.3
  • 61
    • 0026656037 scopus 로고
    • Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic
    • J.-L. Galzi, A. Devillers-Thiery, N. Hussy, S. Bertrand, J.-P. Changeux, and D. Bertrand Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic Nature 359 1992 500 505
    • (1992) Nature , vol.359 , pp. 500-505
    • Galzi, J.-L.1    Devillers-Thiery, A.2    Hussy, N.3    Bertrand, S.4    Changeux, J.-P.5    Bertrand, D.6
  • 62
    • 0033916254 scopus 로고    scopus 로고
    • M2 pore mutations convert the glycine receptor channel from being anion- to cation-selective
    • A. Keramidas, A.J. Moorhouse, C.R. French, P.R. Schofield, and P.H. Barry M2 pore mutations convert the glycine receptor channel from being anion- to cation-selective Biophys. J. 79 2000 247 259
    • (2000) Biophys. J. , vol.79 , pp. 247-259
    • Keramidas, A.1    Moorhouse, A.J.2    French, C.R.3    Schofield, P.R.4    Barry, P.H.5
  • 63
    • 0035815730 scopus 로고    scopus 로고
    • Conversion of the ion selectivity of the 5-HT(3a) receptor from cationic to anionic reveals a conserved feature of the ligand-gated ion channel superfamily
    • M.J. Gunthorpe, and S.C. Lummis Conversion of the ion selectivity of the 5-HT(3a) receptor from cationic to anionic reveals a conserved feature of the ligand-gated ion channel superfamily J. Biol. Chem. 276 2001 10977 10983
    • (2001) J. Biol. Chem. , vol.276 , pp. 10977-10983
    • Gunthorpe, M.J.1    Lummis, S.C.2
  • 65
    • 0041806486 scopus 로고    scopus 로고
    • A cytoplasmic region determines single channel conductance in 5-HT3 receptors
    • S.P. Kelley, J.I. Dunlop, E.F. Kirkness, J.J. Lambert, and J.A. Peters A cytoplasmic region determines single channel conductance in 5-HT3 receptors Nature 424 2003 321 324
    • (2003) Nature , vol.424 , pp. 321-324
    • Kelley, S.P.1    Dunlop, J.I.2    Kirkness, E.F.3    Lambert, J.J.4    Peters, J.A.5
  • 67
    • 0000631357 scopus 로고
    • Complete mRNA coding sequence of the acetylcholine binding α-subunit of Torpedo marmorata acetylcholine receptor: A model for the transmembrane organization of the polypeptide chain
    • A. Devillers-Thiery, J. Giraudat, M. Bentaboulet, and J.-P. Changeux Complete mRNA coding sequence of the acetylcholine binding α-subunit of Torpedo marmorata acetylcholine receptor: a model for the transmembrane organization of the polypeptide chain Proc. Natl Acad. Sci. USA 80 1983 2067 2071
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 2067-2071
    • Devillers-Thiery, A.1    Giraudat, J.2    Bentaboulet, M.3    Changeux, J.-P.4
  • 68
    • 6344294126 scopus 로고    scopus 로고
    • Phylogenetic conservation of disulfide-linked, dimeric acetylcholine receptor pentamers in southern ocean electric rays
    • M.L. Tierney, K.E. Osborn, P.J. Milburn, M.H.B. Stowell, and S.M. Howitt Phylogenetic conservation of disulfide-linked, dimeric acetylcholine receptor pentamers in southern ocean electric rays J. Expt. Biol. 207 2004 3581 3590
    • (2004) J. Expt. Biol. , vol.207 , pp. 3581-3590
    • Tierney, M.L.1    Osborn, K.E.2    Milburn, P.J.3    Stowell, M.H.B.4    Howitt, S.M.5
  • 69
    • 0023040236 scopus 로고
    • Carbohydrate structures of acetylcholine receptor from Torpedo californica and distribution of oligosaccharides among the subunits
    • H. Nomoto, N. Takahashi, Y. Nagaki, S. Endo, Y. Arata, and K. Hayashi Carbohydrate structures of acetylcholine receptor from Torpedo californica and distribution of oligosaccharides among the subunits Eur. J. Biochem. 157 1986 233 242
    • (1986) Eur. J. Biochem. , vol.157 , pp. 233-242
    • Nomoto, H.1    Takahashi, N.2    Nagaki, Y.3    Endo, S.4    Arata, Y.5    Hayashi, K.6
  • 70
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
    • K. Yonekura, S. Maki-Yonekura, and K. Namba Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy Nature 424 2003 643 650
    • (2003) Nature , vol.424 , pp. 643-650
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3
  • 72
  • 73
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallog. 24 1991 946 950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 74
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representations of macromolecules
    • S.V. Evans SETOR: hardware lighted three-dimensional solid model representations of macromolecules J. Mol. Graph. 11 1993 134 138
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 75
    • 84986486656 scopus 로고
    • A rapid finite difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation
    • A. Nicholls, K. Sharp, and B. Honig A rapid finite difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation J. Comput. Chem. 12 1991 435 445
    • (1991) J. Comput. Chem. , vol.12 , pp. 435-445
    • Nicholls, A.1    Sharp, K.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.