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Volumn 42, Issue 13, 1999, Pages 2364-2372

Solution structure of α-conotoxin ImI by 1H nuclear magnetic resonance

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CONOTOXIN; CONOTOXIN; NICOTINIC AGENT; NICOTINIC RECEPTOR; NICOTINIC RECEPTOR BLOCKING AGENT; UNCLASSIFIED DRUG;

EID: 0033168019     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm990114p     Document Type: Article
Times cited : (57)

References (59)
  • 2
    • 0001021863 scopus 로고
    • Conus peptides as chemical probes for receptors and ion channels
    • Myers, R. A.; Cruz, L. J.; Rivier, J. E.; Olivera, B. M. Conus peptides as chemical probes for receptors and ion channels. Chem. Rev. 1993, 93, 1923-1936.
    • (1993) Chem. Rev. , vol.93 , pp. 1923-1936
    • Myers, R.A.1    Cruz, L.J.2    Rivier, J.E.3    Olivera, B.M.4
  • 8
    • 0030064633 scopus 로고    scopus 로고
    • Comparison of binding mechanisms at cholinergic, serotonergic, glycinergic and GABAergic receptors
    • Aprison, M. H.; Galvez-Ruano, E.; Lipkowitz, K. B. Comparison of binding mechanisms at cholinergic, serotonergic, glycinergic and GABAergic receptors. J. Neurosci. Res. 1996, 43, 127-136.
    • (1996) J. Neurosci. Res. , vol.43 , pp. 127-136
    • Aprison, M.H.1    Galvez-Ruano, E.2    Lipkowitz, K.B.3
  • 9
    • 0025884565 scopus 로고
    • Functional architecture of the nicotinic acetylcholine receptor: From electric organ to brain
    • Galzi, J.; Revah, F.; Bessis, A.; Changeux, J. Functional architecture of the nicotinic acetylcholine receptor: From electric organ to brain. Annu. Rev. Pharmacol. Toxicol. 1991, 31, 37-72.
    • (1991) Annu. Rev. Pharmacol. Toxicol. , vol.31 , pp. 37-72
    • Galzi, J.1    Revah, F.2    Bessis, A.3    Changeux, J.4
  • 10
    • 0028082093 scopus 로고
    • Neuronal acetylcholine receptors that bind α-bungarotoxin mediate neurite retraction in a calcium-dependent manner
    • Pugh, P. C.; Berg, D. K. Neuronal acetylcholine receptors that bind α-bungarotoxin mediate neurite retraction in a calcium-dependent manner. J. Neurosci. 1994, 14, 889-896.
    • (1994) J. Neurosci. , vol.14 , pp. 889-896
    • Pugh, P.C.1    Berg, D.K.2
  • 11
    • 0029096914 scopus 로고
    • Nicotine enhancement of fast excitatory synaptic transmission in CNS by presynaptic receptors
    • McGehee, D. S.; Heath, M. J. S.; Gelber, S.; Devay, P.; Role, L. W. Nicotine enhancement of fast excitatory synaptic transmission in CNS by presynaptic receptors. Science 1995, 269, 1692-1696.
    • (1995) Science , vol.269 , pp. 1692-1696
    • McGehee, D.S.1    Heath, M.J.S.2    Gelber, S.3    Devay, P.4    Role, L.W.5
  • 12
    • 0028981913 scopus 로고
    • α-Conotoxin ImI exhibits subtype-specific nicotinic acetylcholine receptor blockade: Preferential inhibition of homomeric α7 and α9 receptors
    • Johnson, D. S.; Martinez, J.; Elgoyhen, A. B.; Heinemann, S. F.; McIntosh, J. M. α-Conotoxin ImI exhibits subtype-specific nicotinic acetylcholine receptor blockade: Preferential inhibition of homomeric α7 and α9 receptors. Mol. Pharmacol. 1995, 48, 194-199.
    • (1995) Mol. Pharmacol. , vol.48 , pp. 194-199
    • Johnson, D.S.1    Martinez, J.2    Elgoyhen, A.B.3    Heinemann, S.F.4    McIntosh, J.M.5
  • 13
    • 0030175612 scopus 로고    scopus 로고
    • Nicotinic receptors in the development and modulation of CNS synapses
    • Role, L. W.; Berg, D. K. Nicotinic receptors in the development and modulation of CNS synapses. Neuron 1996, 16, 1077-1085.
    • (1996) Neuron , vol.16 , pp. 1077-1085
    • Role, L.W.1    Berg, D.K.2
  • 14
    • 12644303225 scopus 로고    scopus 로고
    • Linkage of a neurophysiological deficit in schizophrenia to a chromosome 15 locus
    • Freedman, R.; Byerley, W. Linkage of a neurophysiological deficit in schizophrenia to a chromosome 15 locus. Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 587-592.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 587-592
    • Freedman, R.1    Byerley, W.2
  • 15
    • 0027160989 scopus 로고
    • A role for the nicotinic α-bungarotoxin receptor in neurite outgrowth in PC12 cells
    • Chan, J.; Quik, M. A role for the nicotinic α-bungarotoxin receptor in neurite outgrowth in PC12 cells. Neuroscience 1993, 56, 441-451.
    • (1993) Neuroscience , vol.56 , pp. 441-451
    • Chan, J.1    Quik, M.2
  • 16
    • 0031450275 scopus 로고    scopus 로고
    • Neuronal nicotinic acetylcholine receptors as targets for drug discovery
    • Holladay, M. W.; Dart, M. J.; Lynch, J. K. Neuronal nicotinic acetylcholine receptors as targets for drug discovery. J. Med. Chem. 1997, 40, 4169-4194.
    • (1997) J. Med. Chem. , vol.40 , pp. 4169-4194
    • Holladay, M.W.1    Dart, M.J.2    Lynch, J.K.3
  • 17
    • 0027506299 scopus 로고
    • Nicotinic acetylcholine receptor at 9 Å resolution
    • Unwin, N. Nicotinic acetylcholine receptor at 9 Å resolution. J. Mol. Biol. 1993, 229, 1101-1124.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1101-1124
    • Unwin, N.1
  • 18
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • Unwin, N. Acetylcholine receptor channel imaged in the open state. Nature 1995, 373, 37-43.
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 19
    • 0024319437 scopus 로고
    • Solution structures of α-Conotoxin G1 determined by two-dimensional NMR spectroscopy
    • Pardi, A.; Galdes, A.; Florance, J.; Maniconte, D. Solution structures of α-Conotoxin G1 determined by two-dimensional NMR spectroscopy. Biochemistry 1989, 28, 5494-5501.
    • (1989) Biochemistry , vol.28 , pp. 5494-5501
    • Pardi, A.1    Galdes, A.2    Florance, J.3    Maniconte, D.4
  • 20
    • 0032079381 scopus 로고    scopus 로고
    • Structure determination of the three disulfide bond isomers of α-conotoxin GI: A model for the role of disulfide bonds in structural stability
    • Gehrmann, J.; Alewood, P. F.; Craik, D. J. Structure determination of the three disulfide bond isomers of α-conotoxin GI: a model for the role of disulfide bonds in structural stability. J. Mol. Biol. 1998, 278, 401-415.
    • (1998) J. Mol. Biol. , vol.278 , pp. 401-415
    • Gehrmann, J.1    Alewood, P.F.2    Craik, D.J.3
  • 22
    • 0031469571 scopus 로고    scopus 로고
    • Three-dimensional solution structure of α-Conotoxin MII, an α3β2 neuronal nicotinic acetylcholine receptor-targeted ligand
    • Shon, K.-J.; Koerber, S. C.; Rivier, J. E.; Olivera, B. M.; McIntosh, J. M. Three-dimensional solution structure of α-Conotoxin MII, an α3β2 neuronal nicotinic acetylcholine receptor-targeted ligand. Biochemistry 1997, 36, 15693-15700.
    • (1997) Biochemistry , vol.36 , pp. 15693-15700
    • Shon, K.-J.1    Koerber, S.C.2    Rivier, J.E.3    Olivera, B.M.4    McIntosh, J.M.5
  • 23
    • 0032506167 scopus 로고    scopus 로고
    • Three-dimensional solution structure of α-conotoxin MII by NMR spectroscopy: Effects of solution environment on helicity
    • Hill, J. M.; Oomen, C. J.; Miranda, L. P.; Bingham, J.-P.; Alewood, P. F.; Craik, D. J. Three-dimensional solution structure of α-conotoxin MII by NMR spectroscopy: Effects of solution environment on helicity. Biochemistry 1998, 37, 15621-15630.
    • (1998) Biochemistry , vol.37 , pp. 15621-15630
    • Hill, J.M.1    Oomen, C.J.2    Miranda, L.P.3    Bingham, J.-P.4    Alewood, P.F.5    Craik, D.J.6
  • 24
    • 0029775108 scopus 로고    scopus 로고
    • Three-dimensional structure of the α-conotoxin GI at 1.2 Å resolution
    • Guddat, L. W.; Martin, J. A.; Shan, L.; Edmundson, A. B.; Gray, W. R. Three-dimensional structure of the α-conotoxin GI at 1.2 Å resolution. Biochemistry 1996, 35, 11329-11335.
    • (1996) Biochemistry , vol.35 , pp. 11329-11335
    • Guddat, L.W.1    Martin, J.A.2    Shan, L.3    Edmundson, A.B.4    Gray, W.R.5
  • 25
    • 0030584684 scopus 로고    scopus 로고
    • The 1.1 Å crystal structure of the neuronal acetylcholine receptor antagonist, α-conotoxin PnIA from Conus pennaceus
    • Hu, S.-H.; Gehrmann, J.; Guddat, L. W.; Alewood, P. F.; Craik, D. J.; Martin, J. L. The 1.1 Å crystal structure of the neuronal acetylcholine receptor antagonist, α-conotoxin PnIA from Conus pennaceus. Structure 1996, 4, 417-423.
    • (1996) Structure , vol.4 , pp. 417-423
    • Hu, S.-H.1    Gehrmann, J.2    Guddat, L.W.3    Alewood, P.F.4    Craik, D.J.5    Martin, J.L.6
  • 26
    • 0030968583 scopus 로고    scopus 로고
    • Crystal structure at 1.1 Å resolution of α-conotoxin PnIB: Comparison with α-conotoxins PnIA and GI
    • Hu, S.-H.; Gehrmann, J.; Alewood, P. F.; Craik, D. J.; Martin, J. L. Crystal structure at 1.1 Å resolution of α-conotoxin PnIB: Comparison with α-conotoxins PnIA and GI. Biochemistry 1997, 36, 11323-11330.
    • (1997) Biochemistry , vol.36 , pp. 11323-11330
    • Hu, S.-H.1    Gehrmann, J.2    Alewood, P.F.3    Craik, D.J.4    Martin, J.L.5
  • 29
    • 0032994494 scopus 로고    scopus 로고
    • Alpha-Conotoxin ImI inhibits the alpha-bungarotoxin-resistant nicotonic response in bovine adrenal chromaffin cells
    • Broxton, N. M.; Down, J. G.; Gehrmann, J.; Alewood, P. F.; Satchell, D. G.; Livett, B. G. Alpha-Conotoxin ImI inhibits the alpha-bungarotoxin-resistant nicotonic response in bovine adrenal chromaffin cells. J. Neurochem. 1999, 72, 1656-1662.
    • (1999) J. Neurochem. , vol.72 , pp. 1656-1662
    • Broxton, N.M.1    Down, J.G.2    Gehrmann, J.3    Alewood, P.F.4    Satchell, D.G.5    Livett, B.G.6
  • 30
    • 0029207339 scopus 로고
    • 'Random Coil' 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG
    • Merutka, G.; Dyson, H. J.; Wright, P. E. 'Random Coil' 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG. J. Biomol. NMR 1995, 5, 14-24.
    • (1995) J. Biomol. NMR , vol.5 , pp. 14-24
    • Merutka, G.1    Dyson, H.J.2    Wright, P.E.3
  • 31
    • 0000936646 scopus 로고
    • 13C NMR spectra of two different molecular conformations of a cyclic pentapeptide
    • 13C NMR spectra of two different molecular conformations of a cyclic pentapeptide. FEBS Lett. 1972, 25, 104-108.
    • (1972) FEBS Lett. , vol.25 , pp. 104-108
    • Wüthrich, K.1    Tun-Kyi, A.2    Schwyzer, R.3
  • 32
    • 0028070557 scopus 로고
    • Torsion angle dynamics: Reduced variable conformational sampling enhances crystallographic structure refinement
    • Rice, L. M.; Brunger, A. T. Torsion angle dynamics: Reduced variable conformational sampling enhances crystallographic structure refinement. Proteins: Struct., Funct., Genet. 1994, 19, 277-290.
    • (1994) Proteins: Struct., Funct., Genet. , vol.19 , pp. 277-290
    • Rice, L.M.1    Brunger, A.T.2
  • 34
    • 0032080235 scopus 로고    scopus 로고
    • Structural elements in alpha-conotoxin ImI essential for binding to neuronal alpha7 receptors
    • Quiram, P. A.; Sine, S. M. Structural elements in alpha-conotoxin ImI essential for binding to neuronal alpha7 receptors. J. Biol. Chem. 1998, 273, 11007-11011.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11007-11011
    • Quiram, P.A.1    Sine, S.M.2
  • 35
    • 0032079457 scopus 로고    scopus 로고
    • Identification of residues in the neuronal α7 acetylcholine receptor that confer selectivity for conotoxin ImI
    • Quiram, P. A.; Sine, S. M. Identification of residues in the neuronal α7 acetylcholine receptor that confer selectivity for conotoxin ImI. J. Biol. Chem. 1998, 273, 11001-11006.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11001-11006
    • Quiram, P.A.1    Sine, S.M.2
  • 36
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A.; Davis, D. G. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 1985, 65, 355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 37
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J.; Meier, B. H.; Bachmann, P.; Ernst, R. R. Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 1979, 71, 4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 38
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar, A.; Ernst, R. R.; Wüthrich, K. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 1980, 95, 1-6.
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wüthrich, K.3
  • 40
    • 33644757144 scopus 로고
    • Correlation of proton and nitrogen-15 chemical shifts by multiple quantum NMR
    • Bax, A.; Griffey, R. H.; Hawkins, B. L. Correlation of proton and nitrogen-15 chemical shifts by multiple quantum NMR. J. Magn. Reson. 1983, 55, 301-315.
    • (1983) J. Magn. Reson. , vol.55 , pp. 301-315
    • Bax, A.1    Griffey, R.H.2    Hawkins, B.L.3
  • 41
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M.; Saudek, V.; Sklenar, V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 1992, 2, 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 44
    • 0000939457 scopus 로고
    • The three-dimensional structure of α1-purothionin in solution: Combined use of nuclear magnetic resonance, distance geometry and restrained molecular dynamics
    • Clore, G. M.; Nilges, M.; Sukuraman, D. K.; Brünger, A. T.; Karplus, M.; Gronenborn, A. M. The three-dimensional structure of α1-purothionin in solution: combined use of nuclear magnetic resonance, distance geometry and restrained molecular dynamics. EMBO J. 1986, 5, 2729-2735.
    • (1986) EMBO J. , vol.5 , pp. 2729-2735
    • Clore, G.M.1    Nilges, M.2    Sukuraman, D.K.3    Brünger, A.T.4    Karplus, M.5    Gronenborn, A.M.6
  • 47
    • 0000870109 scopus 로고
    • Three-dimensional structure of proteins determined by molecular dynamics with interproton distance restraints: Application to crambin
    • Brünger, A. T.; Clore, G. M.; Gronenborn, A. M.; Karplus, M. Three-dimensional structure of proteins determined by molecular dynamics with interproton distance restraints: application to crambin. Proc. Natl. Acad. Sci. U.S.A. 1986, 83, 3801-3805.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 3801-3805
    • Brünger, A.T.1    Clore, G.M.2    Gronenborn, A.M.3    Karplus, M.4
  • 48
    • 0030621858 scopus 로고    scopus 로고
    • Torsion angle molecular dynamics as a new efficient tool for NMR structure calculation
    • Stein, E. G.; Rice, L. M.; Brunger, A. T. Torsion angle molecular dynamics as a new efficient tool for NMR structure calculation. J. Magn. Reson. 1997, 124, 154-164.
    • (1997) J. Magn. Reson. , vol.124 , pp. 154-164
    • Stein, E.G.1    Rice, L.M.2    Brunger, A.T.3
  • 49
    • 0023008905 scopus 로고
    • Application of molecular dynamics with interproton distance restraints to three-dimensional protein structure determination. A model study of crambin
    • Clore, G. M.; Brünger, A. T.; Gronenborn, A. M.; Karplus, M. Application of molecular dynamics with interproton distance restraints to three-dimensional protein structure determination. A model study of crambin. J. Mol. Biol. 1986, 191, 523-551.
    • (1986) J. Mol. Biol. , vol.191 , pp. 523-551
    • Clore, G.M.1    Brünger, A.T.2    Gronenborn, A.M.3    Karplus, M.4
  • 51
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF - A program to identify and analyze structural motifs in proteins
    • Hutchinson, E. G.; Thornton, J. M. PROMOTIF - A program to identify and analyze structural motifs in proteins. Protein Sci. 1996, 5, 212-220.
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 52
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structure coordinates
    • Laskowski, R. A.; MacArther, M. W.; Moss, D. S.; Thronton, J. M. PROCHECK: a program to check the stereochemical quality of protein structure coordinates. J. Appl. Crystallogr. 1993, 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArther, M.W.2    Moss, D.S.3    Thronton, J.M.4
  • 53
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald, I. K.; Thornton, J. M. Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 1994, 238, 777-793.
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 59
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J. Biomol. NMR 1995, 5, 67-81.
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Horm, A.3    Hodges, R.S.4    Sykes, B.D.5


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