메뉴 건너뛰기




Volumn 73, Issue 5, 1999, Pages 2158-2166

Identification of a new ligand binding domain in the subunit of the inhibitory glycine receptor

Author keywords

Glycine receptor; Ligand gated ion channel receptor; Mutagenesis; Neurotransmitter

Indexed keywords

BETA ALANINE; GLYCINE RECEPTOR; STRYCHNINE; TAURINE;

EID: 0032692626     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1999.02158.x     Document Type: Article
Times cited : (33)

References (44)
  • 1
    • 0027787023 scopus 로고
    • GABAA receptor needs two homologous domains of the β-subunit for activation by GABA but not by pentobarbital
    • Amin J. and Weiss D. S. (1993) GABAA receptor needs two homologous domains of the β-subunit for activation by GABA but not by pentobarbital. Nature 366, 565-569.
    • (1993) Nature , vol.366 , pp. 565-569
    • Amin, J.1    Weiss, D.S.2
  • 2
    • 0029998387 scopus 로고    scopus 로고
    • A receptor affecting modulation of the channel by ligands of the benzodiazepine binding site
    • A receptor affecting modulation of the channel by ligands of the benzodiazepine binding site. Mol. Pharmacol. 49, 1080-1084.
    • (1996) Mol. Pharmacol. , vol.49 , pp. 1080-1084
    • Buhr, R.1    Baur, R.2    Malherbe, P.3    Sigel, E.4
  • 3
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen C. and Okayama H. (1987) High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7, 2745-2752.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 4
    • 0031468619 scopus 로고    scopus 로고
    • Identification of amino acids contributing to high and low affinity d-tubocurarine sites in the Torpedo nicotinic acetylcholine receptor
    • Chiara D. C. and 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
  • 5
    • 0032548783 scopus 로고    scopus 로고
    • 3H]nicotine photoincorporation in the γ-subunit of the Torpedo nicotinic acetylcholine receptor
    • 3H]nicotine photoincorporation in the γ-subunit of the Torpedo nicotinic acetylcholine receptor. FEBS Lett. 423, 223-226.
    • (1998) FEBS Lett. , vol.423 , pp. 223-226
    • Chiara, D.C.1    Middleton, R.E.2    Cohen, J.B.3
  • 6
    • 0026344986 scopus 로고
    • Structure of the agonist-binding site of the nicotinic acetylcholine receptor
    • Cohen J. B., Sharp S. D., and Liu W. S. (1991) Structure of the agonist-binding site of the nicotinic acetylcholine receptor. 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
  • 7
    • 0032199006 scopus 로고    scopus 로고
    • Binding, gating, affinity and efficacy: The interpretation of structure-activity relationships for agonists and of the effects of mutating receptors
    • Colquhoun D. (1998) Binding, gating, affinity and efficacy: the interpretation of structure-activity relationships for agonists and of the effects of mutating receptors. Br. J. Pharmacol. 125, 924-947.
    • (1998) Br. J. Pharmacol. , vol.125 , pp. 924-947
    • Colquhoun, D.1
  • 9
    • 0032032840 scopus 로고    scopus 로고
    • From muscle endplate to brain synapses: A short history of synapses and agonist-activated ion channels
    • Colquhoun D. and Sakmann B. (1998) From muscle endplate to brain synapses: a short history of synapses and agonist-activated ion channels. Neuron 20, 381-387.
    • (1998) Neuron , vol.20 , pp. 381-387
    • Colquhoun, D.1    Sakmann, B.2
  • 10
    • 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
  • 11
    • 0024278367 scopus 로고
    • Amino acids of the Torpedo marmorata acetylcholine receptor a subunit labeled by a photoaffinity ligand for the acetylcholine binding site
    • Dennis M., Giraudat J., Kotzyba-Hibert F., Goeldner M., Hirth C., Chang J. Y., Lazure C., Chretien M., and Changeux J. P. (1988) Amino acids of the Torpedo marmorata acetylcholine receptor a 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
  • 12
    • 0027522236 scopus 로고
    • Functional architecture of the nicotinic acetylcholine receptor: A prototype of ligand-gated ion channels
    • Devillers-Thiery A., Galzi J. L., Eisele J. L., Bertrand S., Bertrand D., and Changeux J. P. (1993) Functional architecture of the nicotinic acetylcholine receptor: a prototype of ligand-gated ion channels. J. Membr. Biol. 136, 97-112.
    • (1993) J. Membr. Biol. , vol.136 , pp. 97-112
    • Devillers-Thiery, A.1    Galzi, J.L.2    Eisele, J.L.3    Bertrand, S.4    Bertrand, D.5    Changeux, J.P.6
  • 14
    • 0029046913 scopus 로고
    • Neuronal nicotinic receptors: Molecular organization and regulations
    • Galzi J.-L. and Changeux J.-P. (1995) Neuronal nicotinic receptors: molecular organization and regulations. Neuropharmacology 34, 563-582.
    • (1995) Neuropharmacology , vol.34 , pp. 563-582
    • Galzi, J.-L.1    Changeux, J.-P.2
  • 15
    • 0025346780 scopus 로고
    • Identification of a novel amino acid α-tyrosine 93 within the cholinergic ligand-binding sites of the acetylcholine receptor by photoaffinity labeling
    • Galzi J.-L., Revah F., Black D., Goeldner M., Hirth C., and Changeux J.-P. (1990) Identification of a novel amino acid α-tyrosine 93 within the cholinergic ligand-binding sites of the acetylcholine receptor by photoaffinity labeling. 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
  • 16
    • 0025985732 scopus 로고
    • Functional significance of aromatic amino acids from three peptide loops of the α7 neuronal receptor site investigated by site-directed mutagenesis
    • Galzi J.-L., Bertrand D., Devillers-Thiery A., Revah F., Bertrand S., and Changeux J.-P. (1991a) Functional significance of aromatic amino acids from three peptide loops of the α7 neuronal receptor site investigated by site-directed mutagenesis. FEBS Lett. 294, 198-202.
    • (1991) FEBS Lett. , vol.294 , pp. 198-202
    • Galzi, J.-L.1    Bertrand, D.2    Devillers-Thiery, A.3    Revah, F.4    Bertrand, S.5    Changeux, J.-P.6
  • 17
    • 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. (1991b) 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
  • 18
    • 0001789834 scopus 로고
    • Transient production of proteins using an adenovirus transformed cell line
    • German C. M., Gies D. R., and McRay G. (1990) Transient production of proteins using an adenovirus transformed cell line. DNA Protein Eng. Tech. 2, 3-10.
    • (1990) DNA Protein Eng. Tech. , vol.2 , pp. 3-10
    • German, C.M.1    Gies, D.R.2    McRay, G.3
  • 19
    • 0030902081 scopus 로고    scopus 로고
    • Predicted structure of the extracellular region of ligand-gated ion-channel receptors shows SH2-like and SH3-like domains forming the ligand-binding site
    • Gready J. E., Ranganathan S., Schofield P. R., Matsuo Y., and Nishikawa Y. (1997) Predicted structure of the extracellular region of ligand-gated ion-channel receptors shows SH2-like and SH3-like domains forming the ligand-binding site. Protein Sci. 6, 983-988.
    • (1997) Protein Sci. , vol.6 , pp. 983-988
    • Gready, J.E.1    Ranganathan, S.2    Schofield, P.R.3    Matsuo, Y.4    Nishikawa, Y.5
  • 20
    • 0025095280 scopus 로고
    • Alpha subunit variants of the human glycine receptor: Primary structures, functional expression and chromosomal location of corresponding genes
    • Grenningloh G., Schmieden V., Schofield P. R., Seeburg P. H., Siddique T., Mohandas T. K., Becker C.-M., and Betz H. (1990) Alpha subunit variants of the human glycine receptor: primary structures, functional expression and chromosomal location of corresponding genes. EMBO J. 9, 771-776.
    • (1990) EMBO J. , vol.9 , pp. 771-776
    • Grenningloh, G.1    Schmieden, V.2    Schofield, P.R.3    Seeburg, P.H.4    Siddique, T.5    Mohandas, T.K.6    Becker, C.-M.7    Betz, H.8
  • 21
    • 0019441262 scopus 로고
    • Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membranes
    • 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 membranes. 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
  • 22
    • 0024310210 scopus 로고
    • Effect of GABAergic drugs on motor impairment from ethanol, barbital and lorazepam in rat lines selected for differential sensitivity to ethanol
    • Hellevuo K., Kiianmaa K., and Korpi E. R. (1989) Effect of GABAergic drugs on motor impairment from ethanol, barbital and lorazepam in rat lines selected for differential sensitivity to ethanol. Pharmacol. Biochem. Behav. 34, 399-404.
    • (1989) Pharmacol. Biochem. Behav. , vol.34 , pp. 399-404
    • Hellevuo, K.1    Kiianmaa, K.2    Korpi, E.R.3
  • 23
    • 0024520745 scopus 로고
    • Directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho S. N., Hunt H. D., Horton R. M., Pullen J. K., and Pease L. R. (1989) Directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 24
    • 0021132711 scopus 로고
    • Identification of the alpha subunit half-cystine specifically labeled by an affinity reagent for the acetylcholine receptor binding site
    • Kao P., Dwork A., Kaldany R., Silver M., Wideman J., Stein S., and Karlin A. (1984) Identification of the alpha subunit half-cystine specifically labeled by an affinity reagent for the acetylcholine receptor binding site. J. Biol. Chem. 259, 11662-11665.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11662-11665
    • Kao, P.1    Dwork, A.2    Kaldany, R.3    Silver, M.4    Wideman, J.5    Stein, S.6    Karlin, A.7
  • 25
    • 0027392921 scopus 로고
    • Benzodiazepine-induced motor impairment linked to point mutation in cerebellar GABAA receptor
    • Korpi E. R., Kleingoor C., Kettenmann H., and Seeburg P. H. (1993) Benzodiazepine-induced motor impairment linked to point mutation in cerebellar GABAA receptor. Nature 361, 356-359.
    • (1993) Nature , vol.361 , pp. 356-359
    • Korpi, E.R.1    Kleingoor, C.2    Kettenmann, H.3    Seeburg, P.H.4
  • 26
    • 0025648026 scopus 로고
    • A single amino acid exchange alters the pharmacology of neonatal rat glycine receptor subunit
    • Kuhse J., Schmieden V., and Betz H. (1990) A single amino acid exchange alters the pharmacology of neonatal rat glycine receptor subunit. Neuron 5, 867-873.
    • (1990) Neuron , vol.5 , pp. 867-873
    • Kuhse, J.1    Schmieden, V.2    Betz, H.3
  • 27
    • 0001202076 scopus 로고
    • Conserved quarternary structure of ligand-gated ion channels: The postsynaptic glycine receptor is a pentamer
    • Langosch D., Thomas L., and Betz H. (1988) Conserved quarternary structure of ligand-gated ion channels: the postsynaptic glycine receptor is a pentamer. Proc. Natl. Acad. Sci. USA 85, 7394-7398.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7394-7398
    • Langosch, D.1    Thomas, L.2    Betz, H.3
  • 28
    • 0032520102 scopus 로고    scopus 로고
    • Properties of human glycine receptors containing the hyperekplexia mutation α1 (K276E), expressed in Xenopus oocytes
    • Lewis T. M., Sivilotti L. G., Colquhoun D., Gardiner R. M., Schoepfer R., and Rees M. (1998) Properties of human glycine receptors containing the hyperekplexia mutation α1 (K276E), expressed in Xenopus oocytes. J. Physiol. (Lond.) 507, 25-40.
    • (1998) J. Physiol. (Lond.) , vol.507 , pp. 25-40
    • Lewis, T.M.1    Sivilotti, L.G.2    Colquhoun, D.3    Gardiner, R.M.4    Schoepfer, R.5    Rees, M.6
  • 30
    • 0026758178 scopus 로고
    • Mutational analysis of ligand-induced activation of the Torpedo acetylcholine receptor
    • O'Leary M. E. and White M. M. (1992) Mutational analysis of ligand-induced activation of the Torpedo acetylcholine receptor. J. Biol. Chem. 267, 8360-8365.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8360-8365
    • O'Leary, M.E.1    White, M.M.2
  • 31
    • 0021751227 scopus 로고
    • Monoclonal antibodies and peptide mapping reveal structural similarities between the subunits of the glycine receptor of rat spinal cord
    • Pfeiffer F., Simler R., Grenningloh G., and Betz H. (1984) Monoclonal antibodies and peptide mapping reveal structural similarities between the subunits of the glycine receptor of rat spinal cord. Proc. Natl. Acad. Sci. USA 81, 7224-7227.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 7224-7227
    • Pfeiffer, F.1    Simler, R.2    Grenningloh, G.3    Betz, H.4
  • 34
    • 0025359413 scopus 로고
    • Location of the strychnine binding site on the 48-kilodalton subunit of the glycine receptor
    • Ruiz-Gomez A., Morato E., Garcia-Calco M., Valdivieso F., and Mayor F. Jr. (1990) Location of the strychnine binding site on the 48-kilodalton subunit of the glycine receptor. Biochemistry 29, 7033-7040.
    • (1990) Biochemistry , vol.29 , pp. 7033-7040
    • Ruiz-Gomez, A.1    Morato, E.2    Garcia-Calco, M.3    Valdivieso, F.4    Mayor F., Jr.5
  • 36
    • 0027977932 scopus 로고
    • Point mutation of glycine receptor α1 subunit in spasmodic mouse affects agonist responses
    • Saul B., Schmieden V., Kling C., Mulhardt C., Gass P., Kuhse J., and Becker C.-M. (1994) Point mutation of glycine receptor α1 subunit in spasmodic mouse affects agonist responses. FEBS Lett. 350, 71-76.
    • (1994) FEBS Lett. , vol.350 , pp. 71-76
    • Saul, B.1    Schmieden, V.2    Kling, C.3    Mulhardt, C.4    Gass, P.5    Kuhse, J.6    Becker, C.-M.7
  • 37
    • 78651007352 scopus 로고
    • pAx and competitive drug antagonism
    • Schild H. O. (1949) pAx and competitive drug antagonism. Br. J. Pharmacol. Chemotker. 4, 277-280.
    • (1949) Br. J. Pharmacol. Chemotker. , vol.4 , pp. 277-280
    • Schild, H.O.1
  • 38
    • 0024438902 scopus 로고
    • Functional expression in Xenopus oocytes of the strychnine binding 48 kD subunit of the inhibitory glycine receptor
    • Schmieden V., Grenningloh G., Schofield P. R., and Betz H. (1989) Functional expression in Xenopus oocytes of the strychnine binding 48 kD subunit of the inhibitory glycine receptor. EMBO J. 8, 695-700.
    • (1989) EMBO J. , vol.8 , pp. 695-700
    • Schmieden, V.1    Grenningloh, G.2    Schofield, P.R.3    Betz, H.4
  • 39
    • 0027424165 scopus 로고
    • Mutation of glycine receptor subunit creates β-alanine receptor responsive to GABA
    • Schmieden V., Kuhse J., and Betz H. (1993) Mutation of glycine receptor subunit creates β-alanine receptor responsive to GABA. Science 262, 256-258.
    • (1993) Science , vol.262 , pp. 256-258
    • Schmieden, V.1    Kuhse, J.2    Betz, H.3
  • 41
    • 0026004411 scopus 로고
    • Mutations affecting agonist sensitivity of the nicotinic acetylcholine receptor
    • Tomaselli G. F., McLaughlin J. T., Jurman M. E., Hawrot E., and Yellen G. (1991) Mutations affecting agonist sensitivity of the nicotinic acetylcholine receptor. Biophys. J. 60, 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    Yellen, G.5
  • 42
    • 0026787189 scopus 로고
    • Distinct agonist-and antagonist-binding sites on the glycine receptor
    • Vandenberg R. J., Handford C. A., and Schofield P. R. (1992a) Distinct agonist-and antagonist-binding sites on the glycine receptor. Neuron 9, 491-496.
    • (1992) Neuron , vol.9 , pp. 491-496
    • Vandenberg, R.J.1    Handford, C.A.2    Schofield, P.R.3
  • 43
    • 0026536645 scopus 로고
    • Antagonism of ligand-gated ion channel receptors: Two domains of the glycine receptor α subunit form the strychnine binding site
    • Vandenberg R. J., French C. R., Barry P. H., Shine J., and Schofield P. R. (1992b) Antagonism of ligand-gated ion channel receptors: two domains of the glycine receptor α subunit form the strychnine binding site. Proc. Natl. Acad. Sci. USA 89, 1765-1769.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 1765-1769
    • Vandenberg, R.J.1    French, C.R.2    Barry, P.H.3    Shine, J.4    Schofield, P.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.