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Volumn 265, Issue 3, 1999, Pages 902-910

How do acetylcholine receptor ligands reach their binding sites

Author keywords

neurotoxin; Binding sites; Membrane fluidity; Nicotinic acetylcholine receptor; Photoaffinity labeling

Indexed keywords

CHOLINERGIC RECEPTOR; NEUROTOXIN; NICOTINIC RECEPTOR;

EID: 0000119680     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00787.x     Document Type: Article
Times cited : (17)

References (36)
  • 1
    • 0030011258 scopus 로고    scopus 로고
    • The emerging three-dimensional structure of a receptor. The nicotinic acetylcholine receptor
    • 1. Hucho, F., Tsetlin, V.I. & Machold, J. (1996) The emerging three-dimensional structure of a receptor. The nicotinic acetylcholine receptor. Eur. J. Biochem. 239, 539-557.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 539-557
    • Hucho, F.1    Tsetlin, V.I.2    Machold, J.3
  • 2
    • 0029593370 scopus 로고
    • Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins
    • 2. Karlin, A. & Akabas, M.H. (1995) Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins. Neuron 15, 1231-1244.
    • (1995) Neuron , vol.15 , pp. 1231-1244
    • Karlin, A.1    Akabas, M.H.2
  • 3
    • 0028807762 scopus 로고
    • The handedness of the subunit arrangement of the nicotinic acetylcholine receptor
    • 3. Machold, J., Weise, C., Utkin, Y., Tsetlin, V. & Hucho, F. (1995) The handedness of the subunit arrangement of the nicotinic acetylcholine receptor. Eur. J. Biochem. 243, 427-430.
    • (1995) Eur. J. Biochem. , vol.243 , pp. 427-430
    • Machold, J.1    Weise, C.2    Utkin, Y.3    Tsetlin, V.4    Hucho, F.5
  • 4
    • 0025308169 scopus 로고
    • D-tubocurarine binding sites are located at the α-γ and α-δ subunit interphases of the nicotinic acetylcholine receptor
    • 4. Pedersen, S.E. & Cohen, J.B. (1990) d-Tubocurarine binding sites are located at the α-γ and α-δ subunit interphases of the nicotinic acetylcholine receptor. Proc. Natl Acad. Sci. USA 87, 2785-2789.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 2785-2789
    • Pedersen, S.E.1    Cohen, J.B.2
  • 5
    • 0027228267 scopus 로고
    • A high-affinity site for acetylcholine occurs close to the alpha-gamma subunit interface of Torpedo nicotinic acetylcholine receptor
    • 5. Dunn, S.M.J., Conti-Tronconi, B.M. & Raftery, M.A. (1993) A high-affinity site for acetylcholine occurs close to the alpha-gamma subunit interface of Torpedo nicotinic acetylcholine receptor. Biochemistry 32, 8616-8621.
    • (1993) Biochemistry , vol.32 , pp. 8616-8621
    • Dunn, S.M.J.1    Conti-Tronconi, B.M.2    Raftery, M.A.3
  • 6
    • 0026669090 scopus 로고
    • Investigation of ligand binding of the nicotinic acetylcholine receptor using photoactivatable derivatives of neurotoxin ii of Naja naja oxiana
    • 6. Kreienkamp, H.-J., Utkin, Y.N., Weise, C., Machold, J., Tsetlin, V.I. & Hucho, F. (1992) Investigation of ligand binding of the nicotinic acetylcholine receptor using photoactivatable derivatives of neurotoxin II of Naja naja oxiana. Biochemistry 31, 8239-8244.
    • (1992) Biochemistry , vol.31 , pp. 8239-8244
    • Kreienkamp, H.-J.1    Utkin, Y.N.2    Weise, C.3    Machold, J.4    Tsetlin, V.I.5    Hucho, F.6
  • 7
    • 0025819979 scopus 로고
    • 3H-nicotine as an agonist photoaffinity label
    • 3H-nicotine as an agonist photoaffinity label. Biochemistry 30, 6987-6997.
    • (1991) Biochemistry , vol.30 , pp. 6987-6997
    • Middleton, R.E.1    Cohen, J.B.2
  • 8
    • 0025346780 scopus 로고
    • Identificationof a novel amino acid α-Tyr93 within the active site of the acetylcholine receptor by photoaffinity labelling: Additional evidence for the three-loop model of the acetylcholine binding sites
    • 8. Galzi, J.L., Revah, F., Black, D., Goeldner, M., Hirth, C. & Changeux, J.-P. (1990) Identificationof a novel amino acid α-Tyr93 within the active site of the acetylcholine receptor by photoaffinity labelling: additional evidence for the three-loop model of the acetylcholine binding sites. J. Biol. Chem. 265, 10430-10437.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10430-10437
    • Galzi, J.L.1    Revah, F.2    Black, D.3    Goeldner, M.4    Hirth, C.5    Changeux, J.-P.6
  • 9
    • 0026344986 scopus 로고
    • 3H-acetylcholine mustard identifies residues in the cation cation binding subsite
    • 3H-acetylcholine mustard identifies residues in the cation cation binding subsite. J. Biol. Chem. 266, 23354-23364.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23354-23364
    • Cohen, J.B.1    Sharp, S.D.2    Liu, W.S.3
  • 10
    • 0024278367 scopus 로고
    • Amino acids of the Torpedo marmorata acetylcholine receptor alpha subunit labeled by a photoaffinity ligand for the acetylcholine binding site
    • 10. Dennis, M., Giraudat, J., Kotzyba-Hibert, F., Goeldner, M., Hirth, C., Chang, J.Y., Lazure, C., Chretien, M. & Changeux, J.-P. (1988) Amino acids of the Torpedo marmorata acetylcholine receptor alpha subunit labeled by a photoaffinity ligand for the acetylcholine binding site. Biochemistry 27, 2346-2357.
    • (1988) Biochemistry , vol.27 , pp. 2346-2357
    • Dennis, M.1    Giraudat, J.2    Kotzyba-Hibert, F.3    Goeldner, M.4    Hirth, C.5    Chang, J.Y.6    Lazure, C.7    Chretien, M.8    Changeux, J.-P.9
  • 11
    • 0029006150 scopus 로고
    • Nicotinic receptor: An allosteric protein specialized for intercellular communication
    • 11. Bertrand, D. & Changeux, J.-P. (1995) Nicotinic receptor: an allosteric protein specialized for intercellular communication. Neurosciences 7, 75-90.
    • (1995) Neurosciences , vol.7 , pp. 75-90
    • Bertrand, D.1    Changeux, J.-P.2
  • 12
    • 0031468619 scopus 로고    scopus 로고
    • Identification of amino acids contributing to high and low affinity d-tubocurarine sites in the torpedo nicotinic acetylcholine receptor
    • 12. Chiara, D.C. & Cohen, J.B. (1997) Identification of amino acids contributing to high and low affinity d-tubocurarine sites in the torpedo nicotinic acetylcholine receptor. J. Biol. Chem. 272, 32940-32950.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32940-32950
    • Chiara, D.C.1    Cohen, J.B.2
  • 13
    • 0343203033 scopus 로고
    • Analysis of ligand binding to the synthetic dodecapeptide 185-196 of the acetylcholine receptor α-subunit
    • 13. Neumann, D., Barchan, D., Fridkin, M. & Fuchs, S. (1986) Analysis of ligand binding to the synthetic dodecapeptide 185-196 of the acetylcholine receptor α-subunit. Proc. Natl Acad. Sci. USA 83, 9250-9253.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 9250-9253
    • Neumann, D.1    Barchan, D.2    Fridkin, M.3    Fuchs, S.4
  • 15
    • 0025719155 scopus 로고
    • Agonist binding site of torpedo electric tissue nicotinic acetylcholine receptor. A negatively charged region of the δ-subunit within 0.9 nm of the α-subunit binding site disulfide
    • 15. Czajkowski, C. & Karlin, A. (1991) Agonist binding site of Torpedo electric tissue nicotinic acetylcholine receptor. A negatively charged region of the δ-subunit within 0.9 nm of the α-subunit binding site disulfide. J. Biol. Chem. 266, 22603-22612.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22603-22612
    • Czajkowski, C.1    Karlin, A.2
  • 16
    • 0027208097 scopus 로고
    • Negatively charged amino acid residues in the nicotinic receptor delta subunit that contribute to the binding of acetylcholine
    • 16. Czajkowski, C., Kaufmann, C. & Karlin, A. (1993) Negatively charged amino acid residues in the nicotinic receptor delta subunit that contribute to the binding of acetylcholine. Proc. Natl Acad. Sci. USA 90, 6285-6289.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6285-6289
    • Czajkowski, C.1    Kaufmann, C.2    Karlin, A.3
  • 17
    • 0028852622 scopus 로고
    • Structure of the nicotinic acetylcholine binding site - Identification of acidic residues in the δ-subunit within 0.9 nm of the α-subunit binding site disulfide
    • 17. Czajkowski, C. & Karlin, A. (1995) Structure of the nicotinic acetylcholine binding site - identification of acidic residues in the δ-subunit within 0.9 nm of the α-subunit binding site disulfide. J. Biol. Chem. 270, 3160-3164.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3160-3164
    • Czajkowski, C.1    Karlin, A.2
  • 18
    • 0029929234 scopus 로고    scopus 로고
    • The contributions of aspartyl residues in the acetylcholine receptor γ and δ subunits to the binding of agonists and competitive antagonists
    • 18. Martin, M., Czajkowski, C. & Karlin, A. (1996) The contributions of aspartyl residues in the acetylcholine receptor γ and δ subunits to the binding of agonists and competitive antagonists. J. Biol. Chem. 271, 13497-13503.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13497-13503
    • Martin, M.1    Czajkowski, C.2    Karlin, A.3
  • 19
    • 0030813536 scopus 로고    scopus 로고
    • Identification of equivalent residues in the gamma, delta and epsilon subunits of the nicotinic acetylcholine receptor that contribute to alpha-bungarotoxin binding
    • 19. Sine, S.M. (1997) Identification of equivalent residues in the gamma, delta and epsilon subunits of the nicotinic acetylcholine receptor that contribute to alpha-bungarotoxin binding. J. Biol. Chem. 272, 23521-23527.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23521-23527
    • Sine, S.M.1
  • 20
    • 0018709807 scopus 로고
    • Epr and fluorescence study of interaction of Naja naja oxiana neurotoxin II and its derivativeswith acetylcholine receptor protein from Torpedo marmorata
    • 20. Tsetlin, V.I., Karlsson, E., Arseniev, A.S., Utkin, Yu. N., Surin, A.M., Pashkov, V.S., Ivanov, V.I., Bystrov, V.F. & Ovchinnikov, Yu. A. (1979) EPR and fluorescence study of interaction of Naja naja oxiana neurotoxin II and its derivativeswith acetylcholine receptor protein from Torpedo marmorata. FEES Lett. 106, 47-52.
    • (1979) FEES Lett. , vol.106 , pp. 47-52
    • Tsetlin, V.I.1    Karlsson, E.2    Arseniev, A.S.3    Utkin, Y.N.4    Surin, A.M.5    Pashkov, V.S.6    Ivanov, V.I.7    Bystrov, V.F.8    Ovchinnikov, Y.A.9
  • 22
    • 0020967564 scopus 로고
    • The sites of neurotoxicity in α-cobratoxin
    • 22. Martin, B.M., Chibber, B.A. & Maelicke, A. (1983) The sites of neurotoxicity in α-cobratoxin. J. Biol. Chem. 258, 8714-8722.
    • (1983) J. Biol. Chem. , vol.258 , pp. 8714-8722
    • Martin, B.M.1    Chibber, B.A.2    Maelicke, A.3
  • 23
    • 84989578425 scopus 로고
    • Selective neurotoxicity
    • Springer, Berlin
    • 23. Hucho, F. (1992) Selective neurotoxicity. In Handbook of Experimental Pharmacology, pp. 577-610. Springer, Berlin.
    • (1992) Handbook of Experimental Pharmacology , pp. 577-610
    • Hucho, F.1
  • 24
    • 0029136193 scopus 로고
    • Toxins as tools in neurochemistry
    • 24. Hucho, F. (1995) Toxins as tools in neurochemistry. Angew. Chem. Int. Ed. English. 34, 39-50.
    • (1995) Angew. Chem. Int. Ed. English , vol.34 , pp. 39-50
    • Hucho, F.1
  • 25
    • 0017811657 scopus 로고
    • Membranes rich in acetylcholine receptor: Characterization and reconstitution to excitable membranes from exogenous lipids
    • 25. Shiebler, W. & Hucho, F. (1978) Membranes rich in acetylcholine receptor: characterization and reconstitution to excitable membranes from exogenous lipids. Eur. J. Biochem. 85, 55-63.
    • (1978) Eur. J. Biochem. , vol.85 , pp. 55-63
    • Shiebler, W.1    Hucho, F.2
  • 26
    • 0018780571 scopus 로고
    • Preparation of right-side-out, acetylcholine receptor enriched intact vesicles from Torpedo californica electroplaque membranes
    • 26. Hartig, P. & Raftery, M. (1979) Preparation of right-side-out, acetylcholine receptor enriched intact vesicles from Torpedo californica electroplaque membranes. Biochemistry 18, 1146-1150.
    • (1979) Biochemistry , vol.18 , pp. 1146-1150
    • Hartig, P.1    Raftery, M.2
  • 27
    • 0001091926 scopus 로고    scopus 로고
    • Interactions of the nicotinic acetylcholine receptor transmembrane segments with the lipid bilayer in native receptor-rich membranes
    • 27. Dreger, M., Krauss, M., Herrmann, A. & Hucho, F. (1997) Interactions of the nicotinic acetylcholine receptor transmembrane segments with the lipid bilayer in native receptor-rich membranes. Biochemistry 36, 839-847.
    • (1997) Biochemistry , vol.36 , pp. 839-847
    • Dreger, M.1    Krauss, M.2    Herrmann, A.3    Hucho, F.4
  • 30
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels
    • 30. Schevchenko, A., Wilm, M., Vorm, O. & Mann, M. (1996) Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels. Anal. Chem. 68, 850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Schevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • 31. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0025017308 scopus 로고
    • Nonequivalenee of alpha-bungarotoxin binding sites in the native nicotinic receptor molecule
    • 32. Conti-Tronconi, B.M., Tang, F., Walgrave, S. & Gallagher, W. (1990) Nonequivalenee of alpha-bungarotoxin binding sites in the native nicotinic receptor molecule. Biochemistry 29, 1046-1054.
    • (1990) Biochemistry , vol.29 , pp. 1046-1054
    • Conti-Tronconi, B.M.1    Tang, F.2    Walgrave, S.3    Gallagher, W.4
  • 33
    • 0021352689 scopus 로고
    • Fluorescence energy transfer between cobra alpha-toxin molecules bound to the acetylcholine receptor
    • 33. Johnson, D.A., Voet, J.G. & Taylor, P. (1984) Fluorescence energy transfer between cobra alpha-toxin molecules bound to the acetylcholine receptor. J. Biol. Chem. 259, 5717-5725.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5717-5725
    • Johnson, D.A.1    Voet, J.G.2    Taylor, P.3
  • 34
    • 0029114531 scopus 로고
    • Photolabelling reveals proximity of the α-neurotoxin binding site to the M2-helix of the ion channel in the nicotinic acetylcholine receptor
    • 35. Machold, J., Utkin, Y., Kirsch, D., Kaufmann, R., Tsetlin, V. & Hucho, F. (1995) Photolabelling reveals proximity of the α-neurotoxin binding site to the M2-helix of the ion channel in the nicotinic acetylcholine receptor. Proc. Natl Acad. Sci. USA 92, 7282-7286.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 7282-7286
    • Machold, J.1    Utkin, Y.2    Kirsch, D.3    Kaufmann, R.4    Tsetlin, V.5    Hucho, F.6
  • 35
    • 0022943266 scopus 로고
    • The crystal structure of alpha-bungarotoxin at 2.5 a resolution: Relation to solution structure and binding to acetylcholine receptor
    • 36. Love, R.A. & Stroud, R.M. (1986) The crystal structure of alpha-bungarotoxin at 2.5 A resolution: relation to solution structure and binding to acetylcholine receptor. Protein Eng. 1, 37-46.
    • (1986) Protein Eng. , vol.1 , pp. 37-46
    • Love, R.A.1    Stroud, R.M.2
  • 36
    • 0027203297 scopus 로고
    • New photolabelling and crosslinking methods
    • 37. Brunner, J. (1993) New photolabelling and crosslinking methods. Annu. Rev. Biochem. 62, 483-514.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 483-514
    • Brunner, J.1


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