메뉴 건너뛰기




Volumn 44, Issue 25, 2005, Pages 9140-9149

The loop C region of the murine 5-HT3A receptor contributes to the differential actions of 5-hydroxytryptamine and m-chlorophenylbiguanide

Author keywords

[No Author keywords available]

Indexed keywords

BIOASSAY; CHEMICAL BONDS; ELECTRIC POTENTIAL; ELECTRODES; MUTAGENESIS; PROTEINS;

EID: 21944438618     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050661e     Document Type: Article
Times cited : (21)

References (46)
  • 3
    • 0034212292 scopus 로고    scopus 로고
    • Localization of agonist and competitive antagonist binding sites on nicotinic acetylcholine receptors
    • Arias, H. R. (2000) Localization of agonist and competitive antagonist binding sites on nicotinic acetylcholine receptors, Neurochem. Int. 36, 595-645.
    • (2000) Neurochem. Int. , vol.36 , pp. 595-645
    • Arias, H.R.1
  • 4
    • 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. (2001) Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors, Nature 411, 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
  • 18
    • 0030020996 scopus 로고    scopus 로고
    • 3 receptor in mammalian NG108-15 cells
    • 3 receptor in mammalian NG108-15 cells. J. Physiol. 490 (Part 3), 679-690.
    • (1996) J. Physiol. , vol.490 , Issue.PART 3 , pp. 679-690
    • Bartrup, J.T.1    Newberry, N.R.2
  • 19
    • 0035449927 scopus 로고    scopus 로고
    • Open probability of homomeric murine 5-HT3A serotonin receptors depends on subunit occupancy
    • Mott, D. D., Erreger, K., Banke, T. G., and Traynelis, S. F. (2001) Open probability of homomeric murine 5-HT3A serotonin receptors depends on subunit occupancy, J. Physiol. 535, 427-443.
    • (2001) J. Physiol. , vol.535 , pp. 427-443
    • Mott, D.D.1    Erreger, K.2    Banke, T.G.3    Traynelis, S.F.4
  • 21
    • 0347626214 scopus 로고    scopus 로고
    • A vertical flow chamber for Xenopus oocyte electrophysiology and automated drug screening
    • Joshi, P. R., Suryanarayanan, A., and Schulte, M. K. (2004) A vertical flow chamber for Xenopus oocyte electrophysiology and automated drug screening, J. Neurosci. Methods 132, 69-79.
    • (2004) J. Neurosci. Methods , vol.132 , pp. 69-79
    • Joshi, P.R.1    Suryanarayanan, A.2    Schulte, M.K.3
  • 23
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice, Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 24
    • 0035838974 scopus 로고    scopus 로고
    • Extending the accuracy limits of prediction for side-chain conformations
    • Xiang, Z., and Honig, B. (2001) Extending the accuracy limits of prediction for side-chain conformations, J. Mol. Biol. 311, 421-430.
    • (2001) J. Mol. Biol. , vol.311 , pp. 421-430
    • Xiang, Z.1    Honig, B.2
  • 25
    • 0037188507 scopus 로고    scopus 로고
    • Evaluating conformational free energies: The colony energy and its application to the problem of loop prediction
    • Xiang, Z., Soto, C. S., and Honig, B. (2002) Evaluating conformational free energies: The colony energy and its application to the problem of loop prediction, Proc. Natl. Acad. Sci. U.S.A. 99, 7432-7437.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 7432-7437
    • Xiang, Z.1    Soto, C.S.2    Honig, B.3
  • 26
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: A program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 27
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald, I. K., and Thornton, J. M. (1994) Satisfying hydrogen bonding potential in proteins, J. Mol. Biol. 238, 777-793.
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 28
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and empirical binding free energy function
    • Morris, G. M., Goodsell, D. S., Hallaway, R. S., Huey, R., Hart, W. E., Belew, R. K., and Olson, A. J. (1998) Automated Docking Using a Lamarckian Genetic Algorithm and Empirical Binding Free Energy Function, J. Comput. Chem. 19, 1639-1662.
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Hallaway, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 30
    • 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
  • 32
    • 0029895146 scopus 로고    scopus 로고
    • Effects of inhalational general anaesthetics on native glycine receptors in rat medullary neurones and recombinant glycine receptors in Xenopus oocytes
    • Downie, D. L., Hall, A. C., Lieb, W. R., and Franks, N. P. (1996) Effects of inhalational general anaesthetics on native glycine receptors in rat medullary neurones and recombinant glycine receptors in Xenopus oocytes, Br. J. Pharmacol. 118, 493-502.
    • (1996) Br. J. Pharmacol. , vol.118 , pp. 493-502
    • Downie, D.L.1    Hall, A.C.2    Lieb, W.R.3    Franks, N.P.4
  • 33
    • 0034725597 scopus 로고    scopus 로고
    • Arg-274 and Leu-277 of the γ-aminobutyric acid type a receptor α2 subunit define agonist efficacy and potency
    • O'Shea, S. M., and Harrison, N. L. (2000) Arg-274 and Leu-277 of the γ-aminobutyric acid type A receptor α2 subunit define agonist efficacy and potency, J. Biol. Chem. 275, 22764-22768.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22764-22768
    • O'Shea, S.M.1    Harrison, N.L.2
  • 35
    • 0028831226 scopus 로고
    • Mutation of an arginine residue in the human glycine receptor transforms β-alanine and taurine from agonists into competitive antagonists
    • Rajendra, S., Lynch, J. W., Pierce, K. D., French, C. R., Barry, P. H., and Schofield, P. R. (1995) Mutation of an arginine residue in the human glycine receptor transforms β-alanine and taurine from agonists into competitive antagonists, Neuron 14, 169-175.
    • (1995) Neuron , vol.14 , pp. 169-175
    • Rajendra, S.1    Lynch, J.W.2    Pierce, K.D.3    French, C.R.4    Barry, P.H.5    Schofield, P.R.6
  • 36
    • 4644265039 scopus 로고    scopus 로고
    • Molecular structure and function of the glycine receptor chloride channel
    • Lynch, J. W. (2004) Molecular structure and function of the glycine receptor chloride channel, Physiol. Rev. 84, 1051-1095.
    • (2004) Physiol. Rev. , vol.84 , pp. 1051-1095
    • Lynch, J.W.1
  • 37
    • 0032938313 scopus 로고    scopus 로고
    • A mutational analysis of the acetylcholine receptor channel transmitter binding site
    • Akk, G., Zhou, M., and Auerbach, A. (1999) A mutational analysis of the acetylcholine receptor channel transmitter binding site, Biophys. J. 76, 207-218.
    • (1999) Biophys. J. , vol.76 , pp. 207-218
    • Akk, G.1    Zhou, M.2    Auerbach, A.3
  • 38
    • 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
  • 39
    • 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
  • 40
    • 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. (2004) Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures, Neuron 41, 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
  • 41
    • 0024278367 scopus 로고
    • Amino acids of the Torpedo marmorata acetylcholine receptor α 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 α 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
  • 42
    • 0021132711 scopus 로고
    • Identification of the α subunit half-cystine specifically labeled by an affinity reagent for the acetylcholine receptor binding site
    • Kao, P. N., Dwork, A. S., Kaldany, R. R., Silver, M. L., Wideman, J., Stein, S., and Karlin, A. (1984) Identification of the α 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.N.1    Dwork, A.S.2    Kaldany, R.R.3    Silver, M.L.4    Wideman, J.5    Stein, S.6    Karlin, A.7
  • 44
    • 0035141668 scopus 로고    scopus 로고
    • Structure and dynamics of the GABA binding pocket: A narrowing cleft that constricts during activation
    • Wagner, D. A., and Czajkowski, C. (2001) Structure and dynamics of the GABA binding pocket: A narrowing cleft that constricts during activation, J. Neurosci. 21, 67-74.
    • (2001) J. Neurosci. , vol.21 , pp. 67-74
    • Wagner, D.A.1    Czajkowski, C.2
  • 45
    • 0037072311 scopus 로고    scopus 로고
    • Cation-π interactions in ligand recognition by serotonergic (5-HT3A) and nicotinic acetylcholine receptors: The anomalous binding properties of nicotine
    • Beene, D. L., Brandt, G. S., Zhong, W., Zacharias, N. M., Lester, H. Á., and Dougherty, D. A. (2002) Cation-π interactions in ligand recognition by serotonergic (5-HT3A) and nicotinic acetylcholine receptors: The anomalous binding properties of nicotine, Biochemistry 41, 10262-10269.
    • (2002) Biochemistry , vol.41 , pp. 10262-10269
    • Beene, D.L.1    Brandt, G.S.2    Zhong, W.3    Zacharias, N.M.4    Lester, H.Á.5    Dougherty, D.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.