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Volumn 46, Issue 5, 2007, Pages 1194-1204

The role of loop F residues in determining differential d-tubocurarine potencies in mouse and human 5-hydroxytryptamine 3A receptors

Author keywords

[No Author keywords available]

Indexed keywords

CHIMERIC HUMAN RECEPTORS; CURARE POTENCY; MOUSE RESIDUES; MUTANT RECEPTORS;

EID: 33846786975     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0616100     Document Type: Article
Times cited : (14)

References (63)
  • 5
    • 0037835606 scopus 로고    scopus 로고
    • Cloning, physical mapping and expression analysis of the human 5-HT3 serotonin receptor-like genes HTR3C, HTR3D and HTR3E
    • Niesler, B., Frank, B., Kapeller, J., and Rappold, G. A. (2003) Cloning, physical mapping and expression analysis of the human 5-HT3 serotonin receptor-like genes HTR3C, HTR3D and HTR3E, Gene 319, 101-111.
    • (2003) Gene , vol.319 , pp. 101-111
    • Niesler, B.1    Frank, B.2    Kapeller, J.3    Rappold, G.A.4
  • 6
    • 0036703991 scopus 로고    scopus 로고
    • Differential composition of 5-hydroxytryptamine3 receptors synthesized in the rat CNS and peripheral nervous system
    • Morales, M., and Wang, S. D. (2002) Differential composition of 5-hydroxytryptamine3 receptors synthesized in the rat CNS and peripheral nervous system, J. Neurosci. 22, 6732-6741.
    • (2002) J. Neurosci , vol.22 , pp. 6732-6741
    • Morales, M.1    Wang, S.D.2
  • 7
    • 0036117729 scopus 로고    scopus 로고
    • 3 receptor: A model ligand-gated ion channel (review)
    • 3 receptor: a model ligand-gated ion channel (review), Mol. Membr. Biol. 19, 11-26.
    • (2002) Mol. Membr. Biol , vol.19 , pp. 11-26
    • Reeves, D.C.1    Lummis, S.C.R.2
  • 8
    • 0036891560 scopus 로고    scopus 로고
    • The nicotinic receptor ligand binding domain
    • Sine, S. M. (2002) The nicotinic receptor ligand binding domain, J. Neurobiol. 53, 431-446.
    • (2002) J. Neurobiol , vol.53 , pp. 431-446
    • Sine, S.M.1
  • 9
    • 0025308169 scopus 로고
    • d-Tubocurarine binding sites are located at α-γ and α-δ subunit interfaces of the nicotinic acetylcholine receptor
    • Pedersen, S. E., and Cohen, J. B. (1990) d-Tubocurarine binding sites are located at α-γ and α-δ subunit interfaces of the nicotinic acetylcholine receptor, Proc. Natl. Acad. Sci. U. S. A. 87, 2785-2789.
    • (1990) Proc. Natl. Acad. Sci. U. S. A , vol.87 , pp. 2785-2789
    • Pedersen, S.E.1    Cohen, J.B.2
  • 10
    • 0027223874 scopus 로고
    • Selective enhancement of the interaction of curare with the nicotinic acetylcholine receptor
    • Filatov, G. N., Aylwin, M. L., and White, M. M. (1993) Selective enhancement of the interaction of curare with the nicotinic acetylcholine receptor, Mol. Pharmacol. 44, 237-241.
    • (1993) Mol. Pharmacol , vol.44 , pp. 237-241
    • Filatov, G.N.1    Aylwin, M.L.2    White, M.M.3
  • 11
    • 0028292368 scopus 로고
    • Conserved tyrosines in the α subunit of the nicotinic acetylcholine receptor stabilize quaternary ammonium groups of agonists and curariform antagonists
    • Sine, S. M., Quiram, P., Papanikolaou, F., Kreienkamp, H.-J., and Taylor, P. (1994) Conserved tyrosines in the α subunit of the nicotinic acetylcholine receptor stabilize quaternary ammonium groups of agonists and curariform antagonists, J. Biol. Chem. 269, 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
  • 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
    • 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
  • 13
    • 0027482551 scopus 로고
    • Molecular dissection of subunit interfaces in the acetylcholine receptor: Identification of residues that determine curare sensitivity
    • Sine, S. M. (1993) Molecular dissection of subunit interfaces in the acetylcholine receptor: Identification of residues that determine curare sensitivity, Proc. Natl. Acad. Sci. U. S. A. 90, 9436-9440.
    • (1993) Proc. Natl. Acad. Sci. U. S. A , vol.90 , pp. 9436-9440
    • Sine, S.M.1
  • 14
    • 0030868977 scopus 로고    scopus 로고
    • Interaction of d-tubocurarine analogs with mouse nicotinic acetylcholine receptor
    • Papineni, R. V. L., and Pedersen, S. E. (1997) Interaction of d-tubocurarine analogs with mouse nicotinic acetylcholine receptor, J. Biol. Chem. 272, 24891-24898.
    • (1997) J. Biol. Chem , vol.272 , pp. 24891-24898
    • Papineni, R.V.L.1    Pedersen, S.E.2
  • 23
    • 0034084247 scopus 로고    scopus 로고
    • Importance of phenylalanine 107 in agonist recognition by the 5-hydroxytryptamine(3A) receptor
    • Steward, L. J., Boess, F. G., Steele, J. A., Liu, D., Wong, N., and Martin, I. L. (2000) Importance of phenylalanine 107 in agonist recognition by the 5-hydroxytryptamine(3A) receptor, Mol. Pharmacol. 57, 1249-1255.
    • (2000) Mol. Pharmacol , vol.57 , pp. 1249-1255
    • Steward, L.J.1    Boess, F.G.2    Steele, J.A.3    Liu, D.4    Wong, N.5    Martin, I.L.6
  • 30
    • 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
  • 32
    • 0037381989 scopus 로고    scopus 로고
    • Prediction of 5-HT3 receptor agonist-binding residues using homology modeling
    • Reeves, D. C., Sayed, M. F. R., Chau, P.-L., Price, K. L., and Lummis, S. C. R. (2003) Prediction of 5-HT3 receptor agonist-binding residues using homology modeling, Biophys. J. 84, 2338-2344.
    • (2003) Biophys. J , vol.84 , pp. 2338-2344
    • Reeves, D.C.1    Sayed, M.F.R.2    Chau, P.-L.3    Price, K.L.4    Lummis, S.C.R.5
  • 33
    • 27144556414 scopus 로고    scopus 로고
    • Molecular determinants of single-channel conductance and ion selectivity in the Cys-loop family: Insights from the 5-HT3 receptor
    • Peters, J. A., Hales, T. G., and Lambert, J. J. (2005) Molecular determinants of single-channel conductance and ion selectivity in the Cys-loop family: insights from the 5-HT3 receptor, Trends Pharmacol. Sci. 26, 587-594.
    • (2005) Trends Pharmacol. Sci , vol.26 , pp. 587-594
    • Peters, J.A.1    Hales, T.G.2    Lambert, J.J.3
  • 35
    • 0029095767 scopus 로고
    • Molecular cloning of human 5-Hydroxytryptamines receptor: Heterogeneity in distribution and function among species
    • Miyake, A., Mochizuki, S., Takemoto, Y., and Akuzawa, S. (1995) Molecular cloning of human 5-Hydroxytryptamines receptor: heterogeneity in distribution and function among species, Mol. Pharmacol. 48, 407-416.
    • (1995) Mol. Pharmacol , vol.48 , pp. 407-416
    • Miyake, A.1    Mochizuki, S.2    Takemoto, Y.3    Akuzawa, S.4
  • 36
    • 0031886383 scopus 로고    scopus 로고
    • Molecular cloning, functional expression, and pharmacological characterization of 5-hydroxytryptamines receptor cDNA and its splice variants from guinea pig
    • Lankiewicz, S., Lobbitz, S., Lobitz, N., Wetzel, C. H. R., Rupprecht, R., Gisselmann, G., and Hatt, H. (1998) Molecular cloning, functional expression, and pharmacological characterization of 5-hydroxytryptamines receptor cDNA and its splice variants from guinea pig, Mol. Pharmacol. 53, 202-212.
    • (1998) Mol. Pharmacol , vol.53 , pp. 202-212
    • Lankiewicz, S.1    Lobbitz, S.2    Lobitz, N.3    Wetzel, C.H.R.4    Rupprecht, R.5    Gisselmann, G.6    Hatt, H.7
  • 37
    • 0034617383 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of ferret 5-HT-(3) receptor subunit
    • Mochizuki, S., Watanabe, T., Miyake, A., Saito, M., and Furuichi, K. (2000) Cloning, expression, and characterization of ferret 5-HT-(3) receptor subunit, Eur. J. Pharmacol. 399, 97-106.
    • (2000) Eur. J. Pharmacol , vol.399 , pp. 97-106
    • Mochizuki, S.1    Watanabe, T.2    Miyake, A.3    Saito, M.4    Furuichi, K.5
  • 42
    • 0021891887 scopus 로고
    • Effects of site-specific amino acid modification on protein interactions and biological function
    • Ackers, G. K., and Smith, F. R. (1985) Effects of site-specific amino acid modification on protein interactions and biological function, Annu. Rev. Biochem. 54, 597-629.
    • (1985) Annu. Rev. Biochem , vol.54 , pp. 597-629
    • Ackers, G.K.1    Smith, F.R.2
  • 43
    • 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
  • 44
    • 0027136282 scopus 로고
    • Comparitive protein modeling by satisfaction of spatial restraints
    • Sali, A., and Blundell, T. (1993) Comparitive protein modeling by satisfaction of spatial restraints, J. Mol. Biol. 234, 779-815.
    • (1993) J. Mol. Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.2
  • 45
    • 27144473613 scopus 로고    scopus 로고
    • Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations
    • Hansen, S., Sulzenbacher, G., Huxford, T., Marchot, P., Taylor, P., and Bourne, Y. (2005) Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations, EMBO J. 24, 3635-3646.
    • (2005) EMBO J , vol.24 , pp. 3635-3646
    • Hansen, S.1    Sulzenbacher, G.2    Huxford, T.3    Marchot, P.4    Taylor, P.5    Bourne, Y.6
  • 46
    • 0042511005 scopus 로고    scopus 로고
    • A graph-theory algorithm for rapid protein side-chain prediction
    • Cantescu, A. A., Shelenkov, A. A., and Dunbrack, R. L. (2003) A graph-theory algorithm for rapid protein side-chain prediction, Protein Sci. 12, 2001-2014.
    • (2003) Protein Sci , vol.12 , pp. 2001-2014
    • Cantescu, A.A.1    Shelenkov, A.A.2    Dunbrack, R.L.3
  • 47
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • Sippl, M. J. (1993) Recognition of errors in three-dimensional structures of proteins, Proteins 17, 355-362.
    • (1993) Proteins , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 48
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using Lamarckian genetic algorithm and an empirical free energy binding free energy function
    • Morris, G., Goodsell, D., Huey, R., Hart, W., Belew, R., and Olson, A. (1998) Automated docking using Lamarckian genetic algorithm and an empirical free energy binding free energy function, J. Comput. Chem. 19, 1639-1662.
    • (1998) J. Comput. Chem , vol.19 , pp. 1639-1662
    • Morris, G.1    Goodsell, D.2    Huey, R.3    Hart, W.4    Belew, R.5    Olson, A.6
  • 49
    • 49149147973 scopus 로고
    • Iterative partial equalization of orbital electronegativity- A rapid access to atomic charges
    • Gasteiger, J., and Marsili, M. (1980) Iterative partial equalization of orbital electronegativity- A rapid access to atomic charges, Tetrahedron 36, 3219-3228.
    • (1980) Tetrahedron , vol.36 , pp. 3219-3228
    • Gasteiger, J.1    Marsili, M.2
  • 50
    • 1942471391 scopus 로고    scopus 로고
    • Assessing scoring functions for protein-ligand interactions
    • Ferrara, P., Gohlke, H., Price, D. J., Klebe, G., and Brooks, C. L., III (2004) Assessing scoring functions for protein-ligand interactions, J. Med. Chem. 47, 3032-3047.
    • (2004) J. Med. Chem , vol.47 , pp. 3032-3047
    • Ferrara, P.1    Gohlke, H.2    Price, D.J.3    Klebe, G.4    Brooks III, C.L.5
  • 53
    • 0022972430 scopus 로고
    • Location of the ligand-binding sites on the nicotinic acetylcholine receptor α-subunit
    • Pedersen, S. E., Dreyer, E. B., and Cohen, J. B. (1986) Location of the ligand-binding sites on the nicotinic acetylcholine receptor α-subunit, J. Biol. Chem. 261, 13735-13743.
    • (1986) J. Biol. Chem , vol.261 , pp. 13735-13743
    • Pedersen, S.E.1    Dreyer, E.B.2    Cohen, J.B.3
  • 54
    • 0024725677 scopus 로고
    • Molecular basis of the two nonequivalent ligand binding sites of the muscle nicotinic acetylcholine receptor
    • Blount, P., and Merlie, J. P. (1989) Molecular basis of the two nonequivalent ligand binding sites of the muscle nicotinic acetylcholine receptor, Neuron 3, 349-357.
    • (1989) Neuron , vol.3 , pp. 349-357
    • Blount, P.1    Merlie, J.P.2
  • 55
    • 0028316086 scopus 로고
    • Characterization of d-tubocurarine binding site of Torpedo nicotinic acetylcholine receptor
    • O'Leary, M. E., Filatov, G. N., and White, M. M. (1994) Characterization of d-tubocurarine binding site of Torpedo nicotinic acetylcholine receptor, Am. J. Physiol. 266, C648-C653.
    • (1994) Am. J. Physiol , vol.266
    • O'Leary, M.E.1    Filatov, G.N.2    White, M.M.3
  • 56
  • 57
    • 0142090736 scopus 로고    scopus 로고
    • Combinatorial mutations in loops D and F strongly influence responses of the nicotinic acetylcholine receptor to imidacloprid
    • Shimomura, M., Yokota, M., Okumura, M., Matsuda, K., Akamatsu, M., Sattelle, D. V., and Komai, K. (2003) Combinatorial mutations in loops D and F strongly influence responses of the nicotinic acetylcholine receptor to imidacloprid, Brain Res. 991, 71-77.
    • (2003) Brain Res , vol.991 , pp. 71-77
    • Shimomura, M.1    Yokota, M.2    Okumura, M.3    Matsuda, K.4    Akamatsu, M.5    Sattelle, D.V.6    Komai, K.7
  • 58
    • 3042528657 scopus 로고    scopus 로고
    • The structural basis for GTS-21 selectivity between human and rat nicotinic α7 receptors
    • Stokes, C., Papke, J. K. P., Horenstein, N. A., Kem, W. R., McCormack, T. J., and Papke, R. L. (2004) The structural basis for GTS-21 selectivity between human and rat nicotinic α7 receptors, Mol. Pharmacol. 66, 14-24.
    • (2004) Mol. Pharmacol , vol.66 , pp. 14-24
    • Stokes, C.1    Papke, J.K.P.2    Horenstein, N.A.3    Kem, W.R.4    McCormack, T.J.5    Papke, R.L.6
  • 60
    • 0037969585 scopus 로고    scopus 로고
    • 191 segment is involved in GABA binding and channel gating
    • 191 segment is involved in GABA binding and channel gating, J. Biol. Chem. 278, 13166-13172.
    • (2003) J. Biol. Chem , vol.278 , pp. 13166-13172
    • Newell, J.G.1    Czajkowski, C.2
  • 63
    • 0028987938 scopus 로고
    • + channel pore through mutant cycles with a peptide inhibitor
    • + channel pore through mutant cycles with a peptide inhibitor, Science 268, 307-310.
    • (1995) Science , vol.268 , pp. 307-310
    • Hidalgo, P.1    MacKinnon, R.2


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