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Volumn 9, Issue 3, 2009, Pages 306-310

Nicotinic acetylcholine receptors at atomic resolution

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA BUNGAROTOXIN; COBROTOXIN; EPIBATIDINE; NICOTINIC RECEPTOR;

EID: 65749107127     PISSN: 14714892     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.coph.2009.03.005     Document Type: Review
Times cited : (28)

References (30)
  • 1
    • 0036480194 scopus 로고    scopus 로고
    • Emerging structure of the nicotinic acetylcholine receptors
    • The classic comprehensive review describing the progress in high-resolution investigations of AChR.
    • Karlin A. Emerging structure of the nicotinic acetylcholine receptors. Nat Rev Neurosci 3 (2002) 102-114. The classic comprehensive review describing the progress in high-resolution investigations of AChR.
    • (2002) Nat Rev Neurosci , vol.3 , pp. 102-114
    • Karlin, A.1
  • 2
    • 40649084279 scopus 로고    scopus 로고
    • Nicotinic receptors, allosteric proteins and medicine
    • Changeux J.P., and Taly A. Nicotinic receptors, allosteric proteins and medicine. Trends Mol Med 14 (2008) 93-102
    • (2008) Trends Mol Med , vol.14 , pp. 93-102
    • Changeux, J.P.1    Taly, A.2
  • 3
    • 33645302360 scopus 로고    scopus 로고
    • Recent advances in Cys-loop receptor structure and function
    • Sine S.M., and Engel A.G. Recent advances in Cys-loop receptor structure and function. Nature 440 (2006) 448-455
    • (2006) Nature , vol.440 , pp. 448-455
    • Sine, S.M.1    Engel, A.G.2
  • 5
    • 0032478818 scopus 로고    scopus 로고
    • The structure of the potassium channel: molecular basis of K+ conduction and selectivity
    • The first X-ray structure of a voltage dependent ion channel.
    • Doyle D.A., Morais Cabral J., Pfuetzner R.A., Kuo A., Gulbis J.M., Cohen S.L., Chait B.T., and MacKinnon R. The structure of the potassium channel: molecular basis of K+ conduction and selectivity. Science 280 (1998) 69-77. The first X-ray structure of a voltage dependent ion channel.
    • (1998) Science , vol.280 , pp. 69-77
    • Doyle, D.A.1    Morais Cabral, J.2    Pfuetzner, R.A.3    Kuo, A.4    Gulbis, J.M.5    Cohen, S.L.6    Chait, B.T.7    MacKinnon, R.8
  • 6
    • 0035902187 scopus 로고    scopus 로고
    • A glia-derived acetylcholine-binding protein that modulates synaptic transmission
    • A breakthrough discovery of the greatest importance for AChR structural research.
    • Smit A.B., Syed N.I., Schaap D., van Minnen J., Klumperman J., Kits K.S., Lodder H., van der Schors R.C., van Elk R., Sorgedrager B., et al. A glia-derived acetylcholine-binding protein that modulates synaptic transmission. Nature 411 (2001) 261-268. A breakthrough discovery of the greatest importance for AChR structural research.
    • (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    Lodder, H.7    van der Schors, R.C.8    van Elk, R.9    Sorgedrager, B.10
  • 7
    • 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
  • 8
    • 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
  • 9
    • 18444411922 scopus 로고    scopus 로고
    • Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake alpha-neurotoxins and nicotinic receptors
    • Mapping the ligand-binding site with a peptide neurotoxin.
    • Bourne Y., Talley T.T., Hansen S.B., Taylor P., and Marchot P. Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake alpha-neurotoxins and nicotinic receptors. EMBO J 24 (2005) 1512-1522. Mapping the ligand-binding site with a peptide neurotoxin.
    • (2005) EMBO J , vol.24 , pp. 1512-1522
    • Bourne, Y.1    Talley, T.T.2    Hansen, S.B.3    Taylor, P.4    Marchot, P.5
  • 10
    • 1642450641 scopus 로고    scopus 로고
    • Snake and snail toxins acting on nicotinic acetylcholine receptors: fundamental aspects and medical applications
    • Tsetlin V.I., and Hucho F. Snake and snail toxins acting on nicotinic acetylcholine receptors: fundamental aspects and medical applications. FEBS Lett 557 (2004) 9-13
    • (2004) FEBS Lett , vol.557 , pp. 9-13
    • Tsetlin, V.I.1    Hucho, F.2
  • 11
    • 33751049816 scopus 로고    scopus 로고
    • Conotoxins down under
    • Norton R.S., and Olivera B.M. Conotoxins down under. Toxicon 48 (2006) 780-798
    • (2006) Toxicon , vol.48 , pp. 780-798
    • Norton, R.S.1    Olivera, B.M.2
  • 13
    • 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
  • 14
    • 33644870155 scopus 로고    scopus 로고
    • Structural determinants of selective alpha-conotoxin binding to a nicotinic acetylcholine receptor homolog AChBP
    • Ulens C., Hogg R.C., Celie P.H., Bertrand D., Tsetlin V., Smit A.B., and Sixma T.K. Structural determinants of selective alpha-conotoxin binding to a nicotinic acetylcholine receptor homolog AChBP. Proc Natl Acad Sci U S A 103 (2006) 3615-3620
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 3615-3620
    • Ulens, C.1    Hogg, R.C.2    Celie, P.H.3    Bertrand, D.4    Tsetlin, V.5    Smit, A.B.6    Sixma, T.K.7
  • 16
    • 28044455671 scopus 로고    scopus 로고
    • A model for short alpha-neurotoxin bound to nicotinic acetylcholine receptor from Torpedo californica: comparison with long-chain alpha-neurotoxins and alpha-conotoxins
    • MordvintsevDY, Polyak Y.L., Levtsova O.V., Tourleigh Y.V., Kasheverov I.E., Shaitan K.V., Utkin Y.N., and Tsetlin V.I. A model for short alpha-neurotoxin bound to nicotinic acetylcholine receptor from Torpedo californica: comparison with long-chain alpha-neurotoxins and alpha-conotoxins. Comput Biol Chem 29 (2005) 398-411
    • (2005) Comput Biol Chem , vol.29 , pp. 398-411
    • MordvintsevDY1    Polyak, Y.L.2    Levtsova, O.V.3    Tourleigh, Y.V.4    Kasheverov, I.E.5    Shaitan, K.V.6    Utkin, Y.N.7    Tsetlin, V.I.8
  • 17
    • 33748756414 scopus 로고    scopus 로고
    • Alpha-conotoxin analogs with additional positive charge show increased selectivity towards Torpedo californica and some neuronal subtypes of nicotinic acetylcholine receptors
    • Kasheverov I.E., Zhmak M.N., Vulfius C.A., Gorbacheva E.V., Mordvintsev D.Y., Utkin Y.N., van Elk R., Smit A.B., and Tsetlin V.I. Alpha-conotoxin analogs with additional positive charge show increased selectivity towards Torpedo californica and some neuronal subtypes of nicotinic acetylcholine receptors. FEBS J 273 (2006) 4470-4481
    • (2006) FEBS J , vol.273 , pp. 4470-4481
    • Kasheverov, I.E.1    Zhmak, M.N.2    Vulfius, C.A.3    Gorbacheva, E.V.4    Mordvintsev, D.Y.5    Utkin, Y.N.6    van Elk, R.7    Smit, A.B.8    Tsetlin, V.I.9
  • 18
    • 44249110008 scopus 로고    scopus 로고
    • Synthesis and characterization of 125I-alpha-conotoxin ArIB[V11L;V16A], a selective alpha7 nicotinic acetylcholine receptor antagonist
    • Whiteaker P., Marks M.J., Christensen S., Dowell C., Collins A.C., and McIntosh J.M. Synthesis and characterization of 125I-alpha-conotoxin ArIB[V11L;V16A], a selective alpha7 nicotinic acetylcholine receptor antagonist. J Pharmacol Exp Ther 325 (2008) 910-919
    • (2008) J Pharmacol Exp Ther , vol.325 , pp. 910-919
    • Whiteaker, P.1    Marks, M.J.2    Christensen, S.3    Dowell, C.4    Collins, A.C.5    McIntosh, J.M.6
  • 19
    • 4344616080 scopus 로고    scopus 로고
    • Coupling of agonist binding to channel gating in an ACh-binding protein linked to an ion channel
    • An informative model construct visualizing the coupling between ligand-binding site and ion channel.
    • Bouzat C., Gumilar F., Spitzmaul G., Wang H.L., Rayes D., Hansen S.B., Taylor P., and Sine S.M. Coupling of agonist binding to channel gating in an ACh-binding protein linked to an ion channel. Nature 430 (2004) 896-900. An informative model construct visualizing the coupling between ligand-binding site and ion channel.
    • (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    Taylor, P.7    Sine, S.M.8
  • 20
    • 58149193160 scopus 로고    scopus 로고
    • Design and expression of human alpha7 nicotinic acetylcholine receptor extracellular domain mutants with enhanced solubility and ligand-binding properties
    • Zouridakis M., Zisimopoulou P., Eliopoulos E., Poulas K., and Tzartos S.J. Design and expression of human alpha7 nicotinic acetylcholine receptor extracellular domain mutants with enhanced solubility and ligand-binding properties. Biochim Biophys Acta 1794 (2009) 355-366
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 355-366
    • Zouridakis, M.1    Zisimopoulou, P.2    Eliopoulos, E.3    Poulas, K.4    Tzartos, S.J.5
  • 21
    • 34547520128 scopus 로고    scopus 로고
    • Crystal structure of the extracellular domain of nAChR alpha1 bound to alpha-bungarotoxin at 1.94 Å resolution
    • A high-resolution structure of the AChR extracellular domain with a bound antagonist.
    • Dellisanti C.D., Yao Y., Stroud J.C., Wang Z.Z., and Chen L. Crystal structure of the extracellular domain of nAChR alpha1 bound to alpha-bungarotoxin at 1.94 Å resolution. Nat Neurosci 10 (2007) 953-962. A high-resolution structure of the AChR extracellular domain with a bound antagonist.
    • (2007) Nat Neurosci , vol.10 , pp. 953-962
    • Dellisanti, C.D.1    Yao, Y.2    Stroud, J.C.3    Wang, Z.Z.4    Chen, L.5
  • 22
    • 46149085900 scopus 로고    scopus 로고
    • Spontaneous conformational change and toxin binding in alpha7 acetylcholine receptor: insight into channel activation and inhibition
    • Yi M., Tjong H., and Zhou H.X. Spontaneous conformational change and toxin binding in alpha7 acetylcholine receptor: insight into channel activation and inhibition. Proc Natl Acad Sci U S A 105 (2008) 8280-8285
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 8280-8285
    • Yi, M.1    Tjong, H.2    Zhou, H.X.3
  • 23
    • 44449105649 scopus 로고    scopus 로고
    • Effect of cobratoxin binding on the normal mode vibration within acetylcholine binding protein
    • Bertaccini E.J., Lindahl E., Sixma T., and Trudell J.R. Effect of cobratoxin binding on the normal mode vibration within acetylcholine binding protein. J Chem Inf Model 48 (2008) 855-860
    • (2008) J Chem Inf Model , vol.48 , pp. 855-860
    • Bertaccini, E.J.1    Lindahl, E.2    Sixma, T.3    Trudell, J.R.4
  • 24
    • 34548672882 scopus 로고    scopus 로고
    • Structure-guided drug design: conferring selectivity among neuronal nicotinic receptor and acetylcholine-binding protein subtypes
    • Taylor P., Talley T.T., Radic' Z., Hansen S.B., Hibbs R.E., and Shi J. Structure-guided drug design: conferring selectivity among neuronal nicotinic receptor and acetylcholine-binding protein subtypes. Biochem Pharmacol 74 (2007) 1164-1171
    • (2007) Biochem Pharmacol , vol.74 , pp. 1164-1171
    • Taylor, P.1    Talley, T.T.2    Radic', Z.3    Hansen, S.B.4    Hibbs, R.E.5    Shi, J.6
  • 25
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4 Å resolution
    • Unwin N. Refined structure of the nicotinic acetylcholine receptor at 4 Å resolution. J Mol Biol 346 (2005) 967-989
    • (2005) J Mol Biol , vol.346 , pp. 967-989
    • Unwin, N.1
  • 26
    • 27744608733 scopus 로고    scopus 로고
    • Cis-trans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel
    • Lummis S.C., Beene D.L., Lee L.W., Lester H.A., Broadhurst R.W., and Dougherty D.A. Cis-trans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel. Nature 438 (2005) 248-252
    • (2005) Nature , vol.438 , pp. 248-252
    • Lummis, S.C.1    Beene, D.L.2    Lee, L.W.3    Lester, H.A.4    Broadhurst, R.W.5    Dougherty, D.A.6
  • 28
    • 41149168686 scopus 로고    scopus 로고
    • X-ray structure of a prokaryotic pentameric ligand-gated ion channel
    • The first X-ray structure of a ligand gated ion channel, a model with great similarities to the acetylcholine binding protein and the AChR.
    • Hilf R.J., and Dutzler R. X-ray structure of a prokaryotic pentameric ligand-gated ion channel. Nature 452 (2008) 375-379. The first X-ray structure of a ligand gated ion channel, a model with great similarities to the acetylcholine binding protein and the AChR.
    • (2008) Nature , vol.452 , pp. 375-379
    • Hilf, R.J.1    Dutzler, R.2
  • 29
    • 58149267953 scopus 로고    scopus 로고
    • X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation
    • Bocquet N., Nury H., Baaden M., Le Poupon C., Changeux J.P., Delarue M., and Corringer P.J. X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation. Nature 457 (2009) 111-114
    • (2009) Nature , vol.457 , pp. 111-114
    • Bocquet, N.1    Nury, H.2    Baaden, M.3    Le Poupon, C.4    Changeux, J.P.5    Delarue, M.6    Corringer, P.J.7
  • 30
    • 58149242730 scopus 로고    scopus 로고
    • Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel
    • Hilf R.J., and Dutzler R. Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel. Nature 457 (2009) 115-118
    • (2009) Nature , vol.457 , pp. 115-118
    • Hilf, R.J.1    Dutzler, R.2


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