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Volumn 124, Issue 5, 2004, Pages 555-567

Invariant aspartic acid in muscle nicotinic receptor contributes selectively to the kinetics of agonist binding

Author keywords

Acetylcholine receptor; Hydrogen bond; Ligand binding site; Single channel kinetics; Structural model

Indexed keywords

ACETYLCHOLINE; ASPARTIC ACID; BINDING PROTEIN; HYDROXYL GROUP; LIGAND; NICOTINIC RECEPTOR;

EID: 8644263906     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: 10.1085/jgp.200409077     Document Type: Article
Times cited : (38)

References (34)
  • 1
    • 0024349141 scopus 로고
    • An analog of lophotoxin reacts covalently with tyrosine 190 in the α subunit of the nicotinic receptor
    • Abramson, S.N., Y. Li, P. Culver, and P. Taylor. 1989. An analog of lophotoxin reacts covalently with tyrosine 190 in the α subunit of the nicotinic receptor. J. Biol. Chem. 264:12666-12672.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12666-12672
    • Abramson, S.N.1    Li, Y.2    Culver, P.3    Taylor, P.4
  • 2
    • 0035884572 scopus 로고    scopus 로고
    • Aromatics at the murine nicotinic receptor agonist binding site: Mutational analysis of the αY93 and αW149 residues
    • Akk, G. 2001. Aromatics at the murine nicotinic receptor agonist binding site: mutational analysis of the αY93 and αW149 residues. J. Physiol. 535:729-740.
    • (2001) J. Physiol. , vol.535 , pp. 729-740
    • Akk, G.1
  • 3
    • 0032938313 scopus 로고    scopus 로고
    • A mutational analysis of the acetylcholine receptor channel transmitter binding site
    • Akk, G., M. Zhou, and A. Auerbach. 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
  • 4
    • 0035902009 scopus 로고    scopus 로고
    • Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors
    • Brejc, K., W. van Dijk, R. Klassen, M. Schuurmans, J. van der Oost, A. Smit, and T. Sixma. 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.2    Klassen, R.3    Schuurmans, M.4    Van Der Oost, J.5    Smit, A.6    Sixma, T.7
  • 5
    • 1842475289 scopus 로고    scopus 로고
    • Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures
    • Celie, P.H.N., S.E. van Rossum-Fikkert, W.J. van Dijk, K. Brejc, A.B. Smit, and T.K. Sixma. 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.N.1    Van Rossum-Fikkert, S.E.2    Van Dijk, W.J.3    Brejc, K.4    Smit, A.B.5    Sixma, T.K.6
  • 6
    • 0029153305 scopus 로고
    • Activation kinetics of recombinant mouse nicotinic acetylcholine receptors with mutations at α subunit residue tyrosine 190
    • Chen, J., Y. Zhang, G. Akk, S. Sine, and A. Auerbach. 1995. Activation kinetics of recombinant mouse nicotinic acetylcholine receptors with mutations at α subunit residue tyrosine 190. Biophys. J. 69:849-859.
    • (1995) Biophys. J. , vol.69 , pp. 849-859
    • Chen, J.1    Zhang, Y.2    Akk, G.3    Sine, S.4    Auerbach, A.5
  • 7
    • 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
  • 8
    • 0023856335 scopus 로고
    • Activation of ion channels in the frog end-plate by high concentrations of acetylcholine
    • Colquhoun, D., and D.C. Ogden. 1988. Activation of ion channels in the frog end-plate by high concentrations of acetylcholine. J. Physiol. 395:131-159.
    • (1988) J. Physiol. , vol.395 , pp. 131-159
    • Colquhoun, D.1    Ogden, D.C.2
  • 9
    • 0001774017 scopus 로고
    • Fitting and statistical analysis of single channel records
    • B. Sakmann and E. Neher, editors. Plenum Publishing Corp., New York
    • Colquhoun, D., and F. Sigworth. 1983. Fitting and statistical analysis of single channel records. In Single Channel Recording. B. Sakmann and E. Neher, editors. Plenum Publishing Corp., New York. 191-264.
    • (1983) Single Channel Recording , pp. 191-264
    • Colquhoun, D.1    Sigworth, F.2
  • 11
    • 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., J. Giraudat, F. Kotzyba-Hibert, M. Goeldner, C. Hirth, J.Y. Chang, C. Lazure, M. Chretien, and J.P. Changeux. 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
  • 12
    • 0036623799 scopus 로고    scopus 로고
    • Desensitization of diliganded mouse muscle nicotinic acetylcholine receptor channels
    • Elenes, S., and A. Auerbach. 2002. Desensitization of diliganded mouse muscle nicotinic acetylcholine receptor channels. J. Physiol. 541:367-383.
    • (2002) J. Physiol. , vol.541 , pp. 367-383
    • Elenes, S.1    Auerbach, A.2
  • 13
    • 0025346780 scopus 로고
    • Identification of a novel amino acid α-tyrosine 93 within the cholinergic ligands-binding sites of the acetylcholine receptor by photoaffinity labeling. Additional evidence for a three-loop model of the cholinergic ligands-binding sites
    • Galzi, J.L., F. Revah, D. Black, M. Goeldner, C. Hirth, and J.P. Changeux. 1990. Identification of a novel amino acid α-tyrosine 93 within the cholinergic ligands-binding sites of the acetylcholine receptor by photoaffinity labeling. Additional evidence for a three-loop model of the cholinergic ligands-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
  • 14
    • 0037444682 scopus 로고    scopus 로고
    • Properties of the human muscle nicotinic receptor, and of the slow-channel myasthenic syndrome mutant eL221F, inferred from maximum likelihood fits
    • Hatton, C.J., C. Shelley, M. Brydson, D. Beeson, and D. Colquhoun. 2003. Properties of the human muscle nicotinic receptor, and of the slow-channel myasthenic syndrome mutant eL221F, inferred from maximum likelihood fits. J. Physiol. 547:729-760.
    • (2003) J. Physiol. , vol.547 , pp. 729-760
    • Hatton, C.J.1    Shelley, C.2    Brydson, M.3    Beeson, D.4    Colquhoun, D.5
  • 15
    • 0036480194 scopus 로고    scopus 로고
    • The emerging structure of the nicotinic acetylcholine receptors
    • Karlin, A. 2002. The emerging structure of the nicotinic acetylcholine receptors. Nat. Rev. Neurosci. 3:102-114.
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 102-114
    • Karlin, A.1
  • 17
    • 0025999029 scopus 로고
    • Functional differences among nonerythroid anion exchangers expressed in a transfected human cell line
    • Lee, B.S., R.B. Gunn, and R.R. Kopito. 1991. Functional differences among nonerythroid anion exchangers expressed in a transfected human cell line. J. Biol. Chem. 266:11448-11454.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11448-11454
    • Lee, B.S.1    Gunn, R.B.2    Kopito, R.R.3
  • 18
    • 0037172669 scopus 로고    scopus 로고
    • Residues in the ε subunit of the nicotinic acetylcholine receptor interact to confer selectivity of Waglerin-1 for the α-ε subunit interface site
    • Molles, B.E., I. Tsigelny, P. Nguyen, S. Gao, S.M. Sine, and P. Taylor. 2002. Residues in the ε subunit of the nicotinic acetylcholine receptor interact to confer selectivity of Waglerin-1 for the α-ε subunit interface site. Biochemistry. 41:7895-7906.
    • (2002) Biochemistry , vol.41 , pp. 7895-7906
    • Molles, B.E.1    Tsigelny, I.2    Nguyen, P.3    Gao, S.4    Sine, S.M.5    Taylor, P.6
  • 19
    • 15844429136 scopus 로고    scopus 로고
    • Congenital myasthenic syndrome caused by decreased agonist binding affinity due to a mutation in the acetylcholine receptor ε subunit
    • Ohno, K., H.-L. Wang, M. Milone, N. Bren, J.M. Brengman, S. Nakano, P. Quiram, J.N. Pruitt, S.M. Sine, and E.G. Engel. 1996. Congenital myasthenic syndrome caused by decreased agonist binding affinity due to a mutation in the acetylcholine receptor ε subunit. Neuron. 17:157-170.
    • (1996) Neuron , vol.17 , pp. 157-170
    • Ohno, K.1    Wang, H.-L.2    Milone, M.3    Bren, N.4    Brengman, J.M.5    Nakano, S.6    Quiram, P.7    Pruitt, J.N.8    Sine, S.M.9    Engel, E.G.10
  • 20
    • 0027236954 scopus 로고
    • Production of high-titer helper-free retroviruses by transient transfection
    • Pear, W.S., G.P. Nolan, M.L. Scott, and D. Baltimore. 1993. Production of high-titer helper-free retroviruses by transient transfection. Proc. Natl. Acad. Sci. USA. 90:8392-8396.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8392-8396
    • Pear, W.S.1    Nolan, G.P.2    Scott, M.L.3    Baltimore, D.4
  • 21
    • 0002315013 scopus 로고    scopus 로고
    • Structural model of nicotinic acetylcholine receptor isotypes bound to acetylcholine and nicotine
    • Schapira, M., R. Abagyan, and M. Totrov. 2002. Structural model of nicotinic acetylcholine receptor isotypes bound to acetylcholine and nicotine. BMC Struct. Biol. 2:1-8.
    • (2002) BMC Struct. Biol. , vol.2 , pp. 1-8
    • Schapira, M.1    Abagyan, R.2    Totrov, M.3
  • 22
    • 0030061670 scopus 로고    scopus 로고
    • Estimating single channel kinetic parameters from idealized patch clamp data containing missed events
    • Qin, F., A. Auerbach, and F. Sachs. 1996. Estimating single channel kinetic parameters from idealized patch clamp data containing missed events. Biophys. J. 70:264-280.
    • (1996) Biophys. J. , vol.70 , pp. 264-280
    • Qin, F.1    Auerbach, A.2    Sachs, F.3
  • 23
    • 0019215162 scopus 로고
    • Single acetylcholine-activated channels show burst-kinetics in presence of desensitizing concentrations of agonist
    • Sakmann, B., J. Patlak, and E. Neher. 1980. Single acetylcholine- activated channels show burst-kinetics in presence of desensitizing concentrations of agonist. Nature. 286:71-73.
    • (1980) Nature , vol.286 , pp. 71-73
    • Sakmann, B.1    Patlak, J.2    Neher, E.3
  • 24
    • 0036891560 scopus 로고    scopus 로고
    • The nicotinic receptor ligand binding domain
    • Sine, S.M. 2002. The nicotinic receptor ligand binding domain. J. Neurobiol. 3:431-446.
    • (2002) J. Neurobiol. , vol.3 , pp. 431-446
    • Sine, S.M.1
  • 25
    • 0023162262 scopus 로고
    • Activation of acetylcholine receptors in clonal BC3H-1 cells by high concentrations of agonist
    • Sine, S.M., and J.H. Steinbach. 1987. Activation of acetylcholine receptors in clonal BC3H-1 cells by high concentrations of agonist. J. Physiol. 385:325-359.
    • (1987) J. Physiol. , vol.385 , pp. 325-359
    • Sine, S.M.1    Steinbach, J.H.2
  • 26
    • 0025123090 scopus 로고
    • Activation of Torpedo acetylcholine receptors expressed in mouse fibroblasts: Single channel current kinetics reveal distinct agonist binding affinities
    • Sine, S.M., T. Claudio, and F. Sigworth. 1990. Activation of Torpedo acetylcholine receptors expressed in mouse fibroblasts: single channel current kinetics reveal distinct agonist binding affinities. J. Gen. Physiol. 96:395-437.
    • (1990) J. Gen. Physiol. , vol.96 , pp. 395-437
    • Sine, S.M.1    Claudio, T.2    Sigworth, F.3
  • 27
    • 0029087136 scopus 로고
    • Mutation of the acetylcholine receptor α subunit causes a slow-channel myasthenic syndrome by enhancing agonist binding affinity
    • Sine, S.M., K. Ohno, C. Bouzat, A. Auerbach, M. Milone, J.N. Pruitt, and A.C. Engel. 1995. Mutation of the acetylcholine receptor α subunit causes a slow-channel myasthenic syndrome by enhancing agonist binding affinity. Neuron. 15:229-239.
    • (1995) Neuron , vol.15 , pp. 229-239
    • Sine, S.M.1    Ohno, K.2    Bouzat, C.3    Auerbach, A.4    Milone, M.5    Pruitt, J.N.6    Engel, A.C.7
  • 28
    • 0037047296 scopus 로고    scopus 로고
    • Lysine scanning mutagenesis delineates structural model of the nicotinic receptor ligand binding domain
    • Sine, S.M., H.L. Wang, and N. Bren. 2002a. Lysine scanning mutagenesis delineates structural model of the nicotinic receptor ligand binding domain. J. Biol. Chem. 277:29210-29223.
    • (2002) J. Biol. Chem. , vol.277 , pp. 29210-29223
    • Sine, S.M.1    Wang, H.L.2    Bren, N.3
  • 30
    • 0030906795 scopus 로고    scopus 로고
    • Mutation in the Ml domain of the acetylcholine receptor α subunit decreases the rate of agonist dissociation
    • Wang, H.-L., A. Auerbach, N. Bren, K. Ohno, A. Engel, and S. Sine. 1997. Mutation in the Ml domain of the acetylcholine receptor α subunit decreases the rate of agonist dissociation. J. Gen. Physiol. 109:757-766.
    • (1997) J. Gen. Physiol. , vol.109 , pp. 757-766
    • Wang, H.-L.1    Auerbach, A.2    Bren, N.3    Ohno, K.4    Engel, A.5    Sine, S.6
  • 33
    • 0029041254 scopus 로고
    • Activation of recombinant mouse acetylcholine receptors by acetylcholine, carbamylcholine and tetramethylammonium
    • Zhang, Y., J. Chen, and A. Auerbach. 1995. Activation of recombinant mouse acetylcholine receptors by acetylcholine, carbamylcholine and tetramethylammonium. J. Physiol. 486:189-206.
    • (1995) J. Physiol. , vol.486 , pp. 189-206
    • Zhang, Y.1    Chen, J.2    Auerbach, A.3
  • 34
    • 0032514762 scopus 로고    scopus 로고
    • From ab initio quantum mechanics to molecular neurobiology: A cation-pi binding site in the nicotinic receptor
    • Zhong, W., J.P. Gallivan, Y. Zhang, L. Li, H.A. Lester, and D.A. Dougherty. 1998. From ab initio quantum mechanics to molecular neurobiology: a cation-pi binding site in the nicotinic receptor. Proc. Natl. Acad. Sci. USA. 95:12088-12093.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12088-12093
    • Zhong, W.1    Gallivan, J.P.2    Zhang, Y.3    Li, L.4    Lester, H.A.5    Dougherty, D.A.6


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