메뉴 건너뛰기




Volumn 55, Issue 3, 1998, Pages 341-347

Amino acids within residues 181-200 of the nicotinic acetylcholine receptor α1 subunit involved in nicotine binding

Author keywords

Acetylcholine receptor; Amino acids; Fusion proteins; Nicotine; Structure function relationships; Synthetic peptides

Indexed keywords

NICOTINE; NICOTINIC RECEPTOR; SYNTHETIC PEPTIDE;

EID: 0032008103     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(97)00474-7     Document Type: Article
Times cited : (9)

References (40)
  • 1
    • 0029593370 scopus 로고
    • Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins
    • Karlin A, Akabas MH. Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins. Neuron. 15:1995;1231-1244.
    • (1995) Neuron , vol.15 , pp. 1231-1244
    • Karlin, A.1    Akabas, M.H.2
  • 2
    • 0030011258 scopus 로고    scopus 로고
    • The emerging three-dimensional structure of a receptor: The nicotinic acetylcholine receptor
    • Hucho F, Tsetlin VI, Machold J. The emerging three-dimensional structure of a receptor The nicotinic acetylcholine receptor . Eur J Biochem. 239:1996;539-557.
    • (1996) Eur J Biochem , vol.239 , pp. 539-557
    • Hucho, F.1    Tsetlin, V.I.2    Machold, J.3
  • 3
    • 0027228267 scopus 로고
    • A high-affinity site for acetylcholine occurs close to the α-γ subunit interface of Torpedo nicotinic acetylcholine receptor
    • Dunn SMJ, Conti-Tronconi BM, Raftery MA. A high-affinity site for acetylcholine occurs close to the α-γ subunit interface of Torpedo nicotinic acetylcholine receptor. Biochemistry. 32:1993;8616-8621.
    • (1993) Biochemistry , vol.32 , pp. 8616-8621
    • Dunn, S.M.J.1    Conti-Tronconi, B.M.2    Raftery, M.A.3
  • 4
    • 0027482551 scopus 로고
    • Molecular dissection of subunit interfaces in the acetylcholine receptor: Identification of residues that determine curare selectivity
    • Sine SM. Molecular dissection of subunit interfaces in the acetylcholine receptor Identification of residues that determine curare selectivity . Proc Natl Acad Sci USA. 90:1993;9436-9440.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9436-9440
    • Sine, S.M.1
  • 5
    • 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
    • Czajkowski C, Karlin A. 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. 266:1991;22603-22612.
    • (1991) J Biol Chem , vol.266 , pp. 22603-22612
    • Czajkowski, C.1    Karlin, A.2
  • 6
    • 0028852622 scopus 로고
    • Structure of the nicotinic receptor acetylcholine-binding site: Identification of acidic residues in the δ subunit within 0.9 nm of the α subunit-binding site disulfide
    • Czajkowski C, Karlin A. Structure of the nicotinic receptor 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. 270:1995;3160-3164.
    • (1995) J Biol Chem , vol.270 , pp. 3160-3164
    • Czajkowski, C.1    Karlin, A.2
  • 8
    • 0022297959 scopus 로고
    • Determination of the primary amino acid sequence specifying the α-bungarotoxin binding site on the α-subunit of the acetylcholine receptor from Torpedo
    • Wilson PT, Lentz TL, Hawrot E. Determination of the primary amino acid sequence specifying the α-bungarotoxin binding site on the α-subunit of the acetylcholine receptor from Torpedo. Proc Natl Acad Sci USA. 82:1985;8790-8794.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 8790-8794
    • Wilson, P.T.1    Lentz, T.L.2    Hawrot, E.3
  • 9
    • 0024268452 scopus 로고
    • Distribution of α-bungarotoxin binding sites over residues 173-204 of the α-subunit of the acetylcholine receptor
    • Wilson PT, Hawrot E, Lentz TL. Distribution of α-bungarotoxin binding sites over residues 173-204 of the α-subunit of the acetylcholine receptor. Mol Pharmacol. 34:1988;643-650.
    • (1988) Mol Pharmacol , vol.34 , pp. 643-650
    • Wilson, P.T.1    Hawrot, E.2    Lentz, T.L.3
  • 10
    • 0022499114 scopus 로고
    • Mapping of the α-bungarotoxin binding site within the α subunit of the acetylcholine receptor
    • Neumann D, Barchan D, Safran A, Gershoni JM, Fuchs S. Mapping of the α-bungarotoxin binding site within the α subunit of the acetylcholine receptor. Proc Natl Acad Sci USA. 83:1986;3008-3011.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 3008-3011
    • Neumann, D.1    Barchan, D.2    Safran, A.3    Gershoni, J.M.4    Fuchs, S.5
  • 11
    • 0023187905 scopus 로고
    • Synthetic peptides used to locate the α-bungarotoxin binding site and immunogenic regions on α subunits of the nicotinic acetylcholine receptor
    • Ralston S, Sarin V, Thanh HL, Rivier J, Fox JL, Lindstrom J. Synthetic peptides used to locate the α-bungarotoxin binding site and immunogenic regions on α subunits of the nicotinic acetylcholine receptor. Biochemistry. 26:1987;3261-3266.
    • (1987) Biochemistry , vol.26 , pp. 3261-3266
    • Ralston, S.1    Sarin, V.2    Thanh, H.L.3    Rivier, J.4    Fox, J.L.5    Lindstrom, J.6
  • 12
    • 0024281207 scopus 로고
    • Nicotinic acetylcholine receptor: A structural model for α-subunit peptide 188-201, the putative binding site for cholinergic agents
    • Gotti C, Frigerio F, Bolognesi M, Longhi R, Racchetti G, Clementi F. Nicotinic acetylcholine receptor A structural model for α-subunit peptide 188-201, the putative binding site for cholinergic agents . FEBS Lett. 228:1988;118-122.
    • (1988) FEBS Lett , vol.228 , pp. 118-122
    • Gotti, C.1    Frigerio, F.2    Bolognesi, M.3    Longhi, R.4    Racchetti, G.5    Clementi, F.6
  • 13
    • 0023710953 scopus 로고
    • Binding of α-bungarotoxin to synthetic peptides corresponding to residues 173-204 of the α-subunit of Torpedo, calf, and human acetylcholine receptor and restoration of high affinity binding by sodium dodecyl sulfate
    • Wilson PT, Lentz TL. Binding of α-bungarotoxin to synthetic peptides corresponding to residues 173-204 of the α-subunit of Torpedo, calf, and human acetylcholine receptor and restoration of high affinity binding by sodium dodecyl sulfate. Biochemistry. 27:1988;6667-6674.
    • (1988) Biochemistry , vol.27 , pp. 6667-6674
    • Wilson, P.T.1    Lentz, T.L.2
  • 15
    • 0028175814 scopus 로고
    • An α-bungarotoxin-binding sequence on the Torpedo nicotinic acetylcholine receptor α-subunit: Conservative amino acid substitutions reveal side-chain specific interactions
    • McLane KE, Wu X, Conti-Tronconi BM. An α-bungarotoxin-binding sequence on the Torpedo nicotinic acetylcholine receptor α-subunit Conservative amino acid substitutions reveal side-chain specific interactions . Biochemistry. 33:1994;2576-2585.
    • (1994) Biochemistry , vol.33 , pp. 2576-2585
    • McLane, K.E.1    Wu, X.2    Conti-Tronconi, B.M.3
  • 16
    • 0023108720 scopus 로고
    • Mapping the main immunogenic region and toxin-binding site of the nicotinic acetylcholine receptor
    • Barkas T, Mauron A, Roth B, Alliod C, Tzartos SJ, Ballivet M. Mapping the main immunogenic region and toxin-binding site of the nicotinic acetylcholine receptor. Science. 235:1987;77-80.
    • (1987) Science , vol.235 , pp. 77-80
    • Barkas, T.1    Mauron, A.2    Roth, B.3    Alliod, C.4    Tzartos, S.J.5    Ballivet, M.6
  • 17
    • 0025316406 scopus 로고
    • Comparison of the toxin binding sites of the nicotinic acetylcholine receptor from Drosophila to human
    • Ohana B, Gershoni JM. Comparison of the toxin binding sites of the nicotinic acetylcholine receptor from Drosophila to human. Biochemistry. 29:1990;6409-6415.
    • (1990) Biochemistry , vol.29 , pp. 6409-6415
    • Ohana, B.1    Gershoni, J.M.2
  • 18
    • 0026535476 scopus 로고
    • Substitution of Torpedo acetylcholine receptor α1-subunit residues with snake α1- and rat nerve α3-subunit residues in recombinant fusion proteins: Effect on α-bungarotoxin binding
    • Chaturvedi V, Donnelly-Roberts DL, Lentz TL. Substitution of Torpedo acetylcholine receptor α1-subunit residues with snake α1- and rat nerve α3-subunit residues in recombinant fusion proteins Effect on α-bungarotoxin binding . Biochemistry. 31:1992;1370-1375.
    • (1992) Biochemistry , vol.31 , pp. 1370-1375
    • Chaturvedi, V.1    Donnelly-Roberts, D.L.2    Lentz, T.L.3
  • 19
    • 0027431495 scopus 로고
    • Effects of mutations of Torpedo acetylcholine receptor α1 subunit residues 184-200 on α-bungarotoxin binding in a recombinant fusion protein
    • Chaturvedi V, Donnelly-Roberts DL, Lentz TL. Effects of mutations of Torpedo acetylcholine receptor α1 subunit residues 184-200 on α-bungarotoxin binding in a recombinant fusion protein. Biochemistry. 32:1993;9570-9576.
    • (1993) Biochemistry , vol.32 , pp. 9570-9576
    • Chaturvedi, V.1    Donnelly-Roberts, D.L.2    Lentz, T.L.3
  • 20
    • 0028932759 scopus 로고
    • Differential binding of nicotine and α-bungarotoxin to residues 173-204 of the nicotinic acetylcholine receptor α1 subunit
    • Lentz TL. Differential binding of nicotine and α-bungarotoxin to residues 173-204 of the nicotinic acetylcholine receptor α1 subunit. Biochemistry. 34:1995;1316-1322.
    • (1995) Biochemistry , vol.34 , pp. 1316-1322
    • Lentz, T.L.1
  • 21
    • 0026450606 scopus 로고
    • Heterogeneity and regulation of nicotinic acetylcholine receptors
    • Lukas RJ, Bencherif M. Heterogeneity and regulation of nicotinic acetylcholine receptors. Int Rev Neurobiol. 34:1992;25-131.
    • (1992) Int Rev Neurobiol , vol.34 , pp. 25-131
    • Lukas, R.J.1    Bencherif, M.2
  • 22
    • 0029979162 scopus 로고    scopus 로고
    • Pharmacology of nicotine: Addiction and therapeutics
    • Benowitz NL. Pharmacology of nicotine Addiction and therapeutics . Annu Rev Pharmacol Toxicol. 36:1996;597-613.
    • (1996) Annu Rev Pharmacol Toxicol , vol.36 , pp. 597-613
    • Benowitz, N.L.1
  • 23
    • 0016773724 scopus 로고
    • Scatchard plots: Common errors in correction and interpretation
    • Chamness GC, McGuire WL. Scatchard plots Common errors in correction and interpretation . Steroids. 26:1975;538-542.
    • (1975) Steroids , vol.26 , pp. 538-542
    • Chamness, G.C.1    McGuire, W.L.2
  • 24
    • 0016417412 scopus 로고
    • Statistical analysis of radioligand assay data
    • Rodbard D, Frazier GR. Statistical analysis of radioligand assay data. Methods Enzymol. 37:1975;3-22.
    • (1975) Methods Enzymol , vol.37 , pp. 3-22
    • Rodbard, D.1    Frazier, G.R.2
  • 25
    • 0014934202 scopus 로고
    • Structure and activity of acetylcholine
    • Beers WH, Reich E. Structure and activity of acetylcholine. Nature. 228:1970;917-922.
    • (1970) Nature , vol.228 , pp. 917-922
    • Beers, W.H.1    Reich, E.2
  • 26
    • 0021132711 scopus 로고
    • Identification of the α subunit half-cystine specifically labeled by an affinity reagent for the acetylcholine binding site
    • Kao PN, Dwork AJ, Kaldany R-RJ, Silver ML, Wideman J, Stein S, Karlin A. Identification of the α subunit half-cystine specifically labeled by an affinity reagent for the acetylcholine binding site. J Biol Chem. 259:1984;11662-11665.
    • (1984) J Biol Chem , vol.259 , pp. 11662-11665
    • Kao, P.N.1    Dwork, A.J.2    Kaldany, R.-R.J.3    Silver, M.L.4    Wideman, J.5    Stein, S.6    Karlin, A.7
  • 28
    • 0025346780 scopus 로고
    • Identification of a novel amino acid α Tyr 93 within the active site of the acetylcholine receptor by photoaffinity labeling: Additional evidence for a three-loop model of the acetylcholine binding site
    • Galzi JL, Revah F, Black D, Goeldner M, Hirth C, Changeux J-P. Identification of a novel amino acid α Tyr 93 within the active site of the acetylcholine receptor by photoaffinity labeling Additional evidence for a three-loop model of the acetylcholine binding site . J Biol Chem. 265:1990;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
  • 29
    • 0024349141 scopus 로고
    • 190 in the α-subunit of the nicotinic acetylcholine receptor
    • 190 in the α-subunit of the nicotinic acetylcholine receptor. J Biol Chem. 264:1989;12666-12672.
    • (1989) J Biol Chem , vol.264 , pp. 12666-12672
    • Abramson, S.N.1    Li, Y.2    Culver, P.3    Taylor, P.4
  • 30
    • 4244173762 scopus 로고
    • Identification of amino acids contributing to high and low affinity D-tubocurarine (dTC) sites on the Torpedo nicotinic acetylcholine (nAChR) receptor subunits
    • Chiara DC, Cohen JB. Identification of amino acids contributing to high and low affinity D-tubocurarine (dTC) sites on the Torpedo nicotinic acetylcholine (nAChR) receptor subunits. FASEB J. 6:1992;A106.
    • (1992) FASEB J , vol.6 , pp. 106
    • Chiara, D.C.1    Cohen, J.B.2
  • 31
    • 0025884565 scopus 로고
    • Functional architecture of the nicotinic acetylcholine receptor: From electric organ to brain
    • Galzi J-L, Revah F, Bessis A, Changeux J-P. Functional architecture of the nicotinic acetylcholine receptor From electric organ to brain . Annu Rev Pharmacol. 31:1991;37-72.
    • (1991) Annu Rev Pharmacol , vol.31 , pp. 37-72
    • Galzi, J.-L.1    Revah, F.2    Bessis, A.3    Changeux, J.-P.4
  • 32
    • 0025819979 scopus 로고
    • 3H]Nicotine as an agonist photoaffinity label
    • 3H]Nicotine as an agonist photoaffinity label . Biochemistry. 30:1991;6987-6997.
    • (1991) Biochemistry , vol.30 , pp. 6987-6997
    • Middleton, R.E.1    Cohen, J.B.2
  • 33
    • 0026344986 scopus 로고
    • Structure of the agonist-binding site of the nicotinic acetylcholine receptor
    • Cohen JB, Sharp SD, Liu WS. Structure of the agonist-binding site of the nicotinic acetylcholine receptor. J Biol Chem. 266:1991;23354-23364.
    • (1991) J Biol Chem , vol.266 , pp. 23354-23364
    • Cohen, J.B.1    Sharp, S.D.2    Liu, W.S.3
  • 34
    • 0028246033 scopus 로고
    • Ligand-receptor interactions in the nicotinic acetylcholine receptor probed using multiple substitutions at conserved tyrosines on the α subunit
    • Aylwin ML, White MM. Ligand-receptor interactions in the nicotinic acetylcholine receptor probed using multiple substitutions at conserved tyrosines on the α subunit. FEBS Lett. 349:1994;99-103.
    • (1994) FEBS Lett , vol.349 , pp. 99-103
    • Aylwin, M.L.1    White, M.M.2
  • 35
    • 0028292368 scopus 로고
    • Conserved tyrosines in the α subunit of the nicotinic acetylcholine receptor stabilize quaternary ammonium groups of agonists and curariform antagonists
    • Sine SM, Quiram P, Papanikolaou F, Kreienkamp H-J, Taylor P. Conserved tyrosines in the α subunit of the nicotinic acetylcholine receptor stabilize quaternary ammonium groups of agonists and curariform antagonists. J Biol Chem. 269:1994;8808-8816.
    • (1994) J Biol Chem , vol.269 , pp. 8808-8816
    • Sine, S.M.1    Quiram, P.2    Papanikolaou, F.3    Kreienkamp, H.-J.4    Taylor, P.5
  • 37
    • 0022975251 scopus 로고
    • Acetylcholine receptor binding site contains a disulfide cross-link between adjacent half-cystinyl residues
    • Kao PN, Karlin A. Acetylcholine receptor binding site contains a disulfide cross-link between adjacent half-cystinyl residues. J Biol Chem. 261:1986;8085-8088.
    • (1986) J Biol Chem , vol.261 , pp. 8085-8088
    • Kao, P.N.1    Karlin, A.2
  • 38
    • 0025689242 scopus 로고
    • Intrinsic fluorescence of binding-site fragments of the nicotinic acetylcholine receptor: Perturbations produced upon binding α-bungarotoxin
    • Pearce SF, Hawrot E. Intrinsic fluorescence of binding-site fragments of the nicotinic acetylcholine receptor Perturbations produced upon binding α-bungarotoxin . Biochemistry. 29:1990;10649-10659.
    • (1990) Biochemistry , vol.29 , pp. 10649-10659
    • Pearce, S.F.1    Hawrot, E.2
  • 39
    • 0026004411 scopus 로고
    • Mutations affecting agonist sensitivity of the nicotinic acetylcholine receptor
    • Tomaselli GF, McLaughlin JT, Jurman ME, Hawrot E, Yellin G. Mutations affecting agonist sensitivity of the nicotinic acetylcholine receptor. Biophys J. 60:1991;721-727.
    • (1991) Biophys J , vol.60 , pp. 721-727
    • Tomaselli, G.F.1    McLaughlin, J.T.2    Jurman, M.E.3    Hawrot, E.4    Yellin, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.