메뉴 건너뛰기




Volumn 1, Issue 5, 2007, Pages 344-352

Docking of μ-conotoxin GIIIA in the sodium channel outer vestibule

Author keywords

Computer simulation; Ion channel; Molecular model; Mutational analysis; Structural biology; Toxin

Indexed keywords

CONOTOXIN; CONOTOXIN G3; ISOPROTEIN; MESSENGER RNA; SODIUM CHANNEL;

EID: 55749096772     PISSN: 19336950     EISSN: 19336969     Source Type: Journal    
DOI: 10.4161/chan.5112     Document Type: Article
Times cited : (47)

References (54)
  • 1
    • 0022930578 scopus 로고
    • Molecular structure of sodium channels
    • Numa S, Noda M. Molecular structure of sodium channels. Ann NY Acad Sci 1986; 479:338-55.
    • (1986) Ann NY Acad Sci , vol.479 , pp. 338-355
    • Numa, S.1    Noda, M.2
  • 2
    • 0025334586 scopus 로고
    • Pursuing the structure and function of voltage-gated channels
    • Guy HR, Conti F. Pursuing the structure and function of voltage-gated channels. Trends Neurosci 1990; 13:201-6.
    • (1990) Trends Neurosci , vol.13 , pp. 201-206
    • Guy, H.R.1    Conti, F.2
  • 3
    • 0009345298 scopus 로고
    • Purification of the tetrodotoxin-binding component associated with the voltage-sensitive sodium channel from Electrophorus electricus electroplax membranes
    • Agnew WS, Levinson SR, Brabson JS, Raftery MA. Purification of the tetrodotoxin-binding component associated with the voltage-sensitive sodium channel from Electrophorus electricus electroplax membranes. Proc Natl Acad Sci USA 1978; 75:2606-10.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 2606-2610
    • Agnew, W.S.1    Levinson, S.R.2    Brabson, J.S.3    Raftery, M.A.4
  • 4
    • 0015810350 scopus 로고
    • Molecular size of the tetrodotoxin binding site estimated by irradiation inactivation
    • Levinson SR, Ellory JC. Molecular size of the tetrodotoxin binding site estimated by irradiation inactivation. Nat New Biol 1973; 245:122-3.
    • (1973) Nat New Biol , vol.245 , pp. 122-123
    • Levinson, S.R.1    Ellory, J.C.2
  • 5
    • 0025584648 scopus 로고
    • The role of nonprotein domains in the function and synthesis of voltage-gated sodium channels
    • Levinson SR, Thornhill WB, Duch DS, Recio-Pinto E, Urban BW. The role of nonprotein domains in the function and synthesis of voltage-gated sodium channels. Ion Channels 1990; 2:33-64.
    • (1990) Ion Channels , vol.2 , pp. 33-64
    • Levinson, S.R.1    Thornhill, W.B.2    Duch, D.S.3    Recio-Pinto, E.4    Urban, B.W.5
  • 6
    • 0020665772 scopus 로고
    • Principal glycopeptide of the tetrodotoxin/saxitoxin binding protein from Electrophorus electricus: Isolation and partial chemical and physical characterization
    • Miller JA, Agnew WS, Levinson SR. Principal glycopeptide of the tetrodotoxin/saxitoxin binding protein from Electrophorus electricus: Isolation and partial chemical and physical characterization. Biochemistry 1983; 22:462-70.
    • (1983) Biochemistry , vol.22 , pp. 462-470
    • Miller, J.A.1    Agnew, W.S.2    Levinson, S.R.3
  • 7
    • 0346614200 scopus 로고
    • Discrimination of muscle and neuronal Na+-channel subtypes by binding competition between [3H]saxitoxin and m-conotoxins
    • Moczydlowski E, Olivera BM, Gray WR, Strichartz GR. Discrimination of muscle and neuronal Na+-channel subtypes by binding competition between [3H]saxitoxin and m-conotoxins. Proc Natl Acad Sci USA 1986; 83:5321-5.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 5321-5325
    • Moczydlowski, E.1    Olivera, B.M.2    Gray, W.R.3    Strichartz, G.R.4
  • 8
    • 0028180093 scopus 로고
    • The mI skeletal muscle sodium channel: Mutation E403Q eliminates sensitivity to tetrodotoxin but not to m-conotoxins GIIIA and GIIIB
    • Stephan MM, Potts JF, Agnew WS. The mI skeletal muscle sodium channel: Mutation E403Q eliminates sensitivity to tetrodotoxin but not to m-conotoxins GIIIA and GIIIB. J Membr Biol 1994; 137:1-8.
    • (1994) J Membr Biol , vol.137 , pp. 1-8
    • Stephan, M.M.1    Potts, J.F.2    Agnew, W.S.3
  • 9
    • 0032584292 scopus 로고    scopus 로고
    • Predominant interactions between m-conotoxin Arg-13 and the skeletal muscle Na+ channel localized by mutant cycle analysis
    • Chang NS, French RJ, Lipkind GM, Fozzard HA, Dudley Jr S. Predominant interactions between m-conotoxin Arg-13 and the skeletal muscle Na+ channel localized by mutant cycle analysis. Biochemistry 1998; 37:4407-19.
    • (1998) Biochemistry , vol.37 , pp. 4407-4419
    • Chang, N.S.1    French, R.J.2    Lipkind, G.M.3    Fozzard, H.A.4    Dudley Jr., S.5
  • 10
    • 0028970541 scopus 로고
    • A m-conotoxin-insensitive Na+ channel mutant: Possible localization of a binding site at the outer vestibule
    • Dudley Jr SC, Todt H, Lipkind G, Fozzard HA. A m-conotoxin-insensitive Na+ channel mutant: Possible localization of a binding site at the outer vestibule. Biophys J 1995; 69:1657-65.
    • (1995) Biophys J. , vol.69 , pp. 1657-1665
    • Dudley Jr., S.C.1    Todt, H.2    Lipkind, G.3    Fozzard, H.A.4
  • 11
    • 0030770381 scopus 로고    scopus 로고
    • Pore residues critical for m-CTX binding to rat skeletal muscle Na+ channels revealed by cysteine mutagenesis
    • Li RA, Tsushima RG, Kallen RG, Backx PH. Pore residues critical for m-CTX binding to rat skeletal muscle Na+ channels revealed by cysteine mutagenesis. Biophys J 1997; 73:1874-84.
    • (1997) Biophys J. , vol.73 , pp. 1874-1884
    • Li, R.A.1    Tsushima, R.G.2    Kallen, R.G.3    Backx, P.H.4
  • 12
    • 0035815713 scopus 로고    scopus 로고
    • Clockwise domain arrangement of the sodium channel revealed by m-conotoxin (GIIIA) docking orientation
    • Li RA, Ennis IL, French RJ, Dudley Jr SC, Tomaselli GF, Marban E. Clockwise domain arrangement of the sodium channel revealed by m-conotoxin (GIIIA) docking orientation. J Biol Chem 2001; 276:11072.
    • (2001) J Biol Chem , vol.276 , pp. 11072
    • Li, R.A.1    Ennis, I.L.2    French, R.J.3    Dudley Jr., S.C.4    Tomaselli, G.F.5    Marban, E.6
  • 13
    • 0033756777 scopus 로고    scopus 로고
    • M-conotoxin GIIIA interactions with the voltage-gated Na+ channel predict a clockwise arrangement of the domains
    • Dudley Jr SC, Chang N, Hall J, Lipkind G, Fozzard HA, French RJ. m-conotoxin GIIIA interactions with the voltage-gated Na+ channel predict a clockwise arrangement of the domains. J Gen Physiol 2000; 116:679-90.
    • (2000) J Gen Physiol , vol.116 , pp. 679-690
    • Dudley Jr., S.C.1    Chang, N.2    Hall, J.3    Lipkind, G.4    Fozzard, H.A.5    French, R.J.6
  • 14
    • 0141530983 scopus 로고    scopus 로고
    • Novel interactions identified between m-Conotoxin and the Na+ channel domain i P-loop: Implications for toxin-pore binding geometry
    • Xue T, Ennis IL, Sato K, French RJ, Li RA. Novel interactions identified between m-Conotoxin and the Na+ channel domain I P-loop: Implications for toxin-pore binding geometry. Biophys J 2003; 85:2299-310.
    • (2003) Biophys J. , vol.85 , pp. 2299-2310
    • Xue, T.1    Ennis, I.L.2    Sato, K.3    French, R.J.4    Li, R.A.5
  • 15
    • 33750402366 scopus 로고    scopus 로고
    • A conserved ring of charge in mammalian Na+ channels: A molecular regulator of the outer pore conformation during slow inactivation
    • Xiong W, Farukhi YZ, Tian Y, Disilvestre D, Li RA, Tomaselli GF. A conserved ring of charge in mammalian Na+ channels: A molecular regulator of the outer pore conformation during slow inactivation. J Physiol 2006; 576:739-54.
    • (2006) J Physiol , vol.576 , pp. 739-754
    • Xiong, W.1    Farukhi, Y.Z.2    Tian, Y.3    Disilvestre, D.4    Li, R.A.5    Tomaselli, G.F.6
  • 16
    • 0031443441 scopus 로고    scopus 로고
    • Sodium channel selectivity filter regulates antiarrhythmic drug binding
    • Sunami A, Dudley Jr SC, Fozzard HA. Sodium channel selectivity filter regulates antiarrhythmic drug binding. Proc Natl Acad Sci USA 1997; 94:14126-31.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14126-14131
    • Sunami, A.1    Dudley Jr., S.C.2    Fozzard, H.A.3
  • 17
    • 0035142987 scopus 로고    scopus 로고
    • Specific neosaxitoxin interactions with the Na+ channel outer vestibule determined by mutant cycle analysis
    • Penzotti JL, Lipkind G, Fozzard HA, Dudley Jr SC. Specific neosaxitoxin interactions with the Na+ channel outer vestibule determined by mutant cycle analysis. Biophys J 2001; 80:698-706.
    • (2001) Biophys J. , vol.80 , pp. 698-706
    • Penzotti, J.L.1    Lipkind, G.2    Fozzard, H.A.3    Dudley Jr., S.C.4
  • 19
    • 0037488179 scopus 로고    scopus 로고
    • Conotoxins as sensors of local pH and electrostatic potential in the outer vestibule of the sodium channel
    • Hui K, McIntyre D, French RJ. Conotoxins as sensors of local pH and electrostatic potential in the outer vestibule of the sodium channel. J Gen Physiol 2003; 122:63-79.
    • (2003) J Gen Physiol , vol.122 , pp. 63-79
    • Hui, K.1    McIntyre, D.2    French, R.J.3
  • 20
    • 0036141825 scopus 로고    scopus 로고
    • Electrostatic and steric contributions to block of the skeletal muscle sodium channel by m-conotoxin
    • Hui K, Lipkind G, Fozzard HA, French RJ. Electrostatic and steric contributions to block of the skeletal muscle sodium channel by m-conotoxin. J Gen Physiol 2002; 119:45-54.
    • (2002) J Gen Physiol , vol.119 , pp. 45-54
    • Hui, K.1    Lipkind, G.2    Fozzard, H.A.3    French, R.J.4
  • 22
    • 0028987938 scopus 로고
    • Revealing the architecture of a K+ channel pore through mutant cycles with a peptide inhibitor
    • Hidalgo P, MacKinnon R. Revealing the architecture of a K+ channel pore through mutant cycles with a peptide inhibitor. Science 1995;268:307-310
    • (1995) Science , vol.268 , pp. 307-310
    • Hidalgo, P.1    Mackinnon, R.2
  • 23
    • 0025093185 scopus 로고
    • Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles
    • Serrano L, Horovitz A, Avron B, Bycroft M, Fersht AR. Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles. Biochemistry 1990; 29:9343.
    • (1990) Biochemistry , vol.29 , pp. 9343
    • Serrano, L.1    Horovitz, A.2    Avron, B.3    Bycroft, M.4    Fersht, A.R.5
  • 25
    • 12244288289 scopus 로고    scopus 로고
    • Interactions of the C-11 hydroxyl of tetrodotoxin with the sodium channel outer vestibule
    • Choudhary G, Yotsu-Yamashita M, Shang L, Yasumoto T, Dudley Jr SC. Interactions of the C-11 hydroxyl of tetrodotoxin with the sodium channel outer vestibule. Biophys J 2003; 84:287-94.
    • (2003) Biophys J. , vol.84 , pp. 287-294
    • Choudhary, G.1    Yotsu-Yamashita, M.2    Shang, L.3    Yasumoto, T.4    Dudley Jr., S.C.5
  • 27
    • 0033557181 scopus 로고    scopus 로고
    • Folding-unfolding thermodynamics of a b-heptapeptide from equilibrium simulations
    • Daura X, van Gunsteren WF, Mark AE. Folding-unfolding thermodynamics of a b-heptapeptide from equilibrium simulations. Proteins 1999; 34:269-80.
    • (1999) Proteins , vol.34 , pp. 269-280
    • Daura, X.1    Van Gunsteren, W.F.2    Mark, A.E.3
  • 28
    • 0034682616 scopus 로고    scopus 로고
    • KcsA crystal structure as framework for a molecular model of the Na+ channel pore
    • Lipkind GM, Fozzard HA. KcsA crystal structure as framework for a molecular model of the Na+ channel pore. Biochemistry 2000; 39:8161-70.
    • (2000) Biochemistry , vol.39 , pp. 8161-8170
    • Lipkind, G.M.1    Fozzard, H.A.2
  • 31
    • 0036840108 scopus 로고    scopus 로고
    • Modeling the structure of agitoxin in complex with the Shaker K+ channel: A computational approach based on experimental distance restraints extracted from thermodynamic mutant cycles
    • Eriksson MA, Roux B. Modeling the structure of agitoxin in complex with the Shaker K+ channel: A computational approach based on experimental distance restraints extracted from thermodynamic mutant cycles. Biophys J 2002; 83:2595-609.
    • (2002) Biophys J. , vol.83 , pp. 2595-2609
    • Eriksson, M.A.1    Roux, B.2
  • 32
    • 0029633168 scopus 로고
    • Gromacs - A message-passing parallel molecular-dynamics implementation
    • Berendsen HJC, Vanderspoel D, Vandrunen R. Gromacs - A message-passing parallel molecular-dynamics implementation. Comput Phys Commun 1995; 91:43-56.
    • (1995) Comput Phys Commun , vol.91 , pp. 43-56
    • Berendsen, H.J.C.1    Vanderspoel, D.2    Vandrunen, R.3
  • 33
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl E, Hess B, van der Spoel D. GROMACS 3.0: A package for molecular simulation and trajectory analysis. J Mol Model 2001; 7:306-17.
    • (2001) J Mol Model , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 35
    • 0030999097 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature
    • Berger O, Edholm O, Jahnig F. Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature. Biophys J 1997; 72:2002-13.
    • (1997) Biophys J. , vol.72 , pp. 2002-2013
    • Berger, O.1    Edholm, O.2    Jahnig, F.3
  • 37
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • Hess B, Bekker H, Berendsen HJC, Fraaije J. LINCS: A linear constraint solver for molecular simulations. J Comput Chem 1997; 18:1463-72.
    • (1997) J Comput Chem , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.J.C.3    Fraaije, J.4
  • 38
    • 33846823909 scopus 로고
    • Particle Mesh Ewald: An N-log (N) method for Ewald sums in large systems
    • Daerden T, York D, Pedersen L. Particle Mesh Ewald: An N-log (N) method for Ewald sums in large systems. Journal of Chemical Physics 1993; 98:1463-72.
    • (1993) Journal of Chemical Physics , vol.98 , pp. 1463-1472
    • Daerden, T.1    York, D.2    Pedersen, L.3
  • 41
    • 9144242506 scopus 로고    scopus 로고
    • Sodium channel toxins-receptor targeting and therapeutic potential
    • French RJ, Terlau H. Sodium channel toxins-receptor targeting and therapeutic potential. Curr Med Chem 2004; 11:3053-64.
    • (2004) Curr Med Chem , vol.11 , pp. 3053-3064
    • French, R.J.1    Terlau, H.2
  • 42
    • 61349091827 scopus 로고    scopus 로고
    • An attempt to determine the orientation of m-conotoxin binding to sodium channels by mapping the contributions of individual residues to the voltage dependence of block
    • McArthur JR, French RJ. An attempt to determine the orientation of m-conotoxin binding to sodium channels by mapping the contributions of individual residues to the voltage dependence of block. Biophys J 2007; 178A-A.
    • (2007) Biophys J.
    • McArthur, J.R.1    French, R.J.2
  • 44
    • 0026657359 scopus 로고
    • Action of derivatives of m-conotoxin GIIIA on sodium channels: Single amino acid substitutions in the toxin separately affect association and dissociation rates
    • Becker S, Prusak-Sochaczewski E, Zamponi G, Beck-Sickinger AG, Gordon RD, French RJ. Action of derivatives of m-conotoxin GIIIA on sodium channels: Single amino acid substitutions in the toxin separately affect association and dissociation rates. Biochemistry 1992; 31:8229-38.
    • (1992) Biochemistry , vol.31 , pp. 8229-8238
    • Becker, S.1    Prusak-Sochaczewski, E.2    Zamponi, G.3    Beck-Sickinger, A.G.4    Gordon, R.D.5    French, R.J.6
  • 45
    • 0029417234 scopus 로고
    • Characterizing the m-conotoxin binding site on voltage-sensitive sodium channels with toxin analogs and channel mutations
    • Chahine M, Chen LQ, Fotouhi N, Walsky R, Fry D, Santarelli V, Horn R, Kallen RG. Characterizing the m-conotoxin binding site on voltage-sensitive sodium channels with toxin analogs and channel mutations. Receptors Channels 1995; 3:161-74.
    • (1995) Receptors Channels , vol.3 , pp. 161-174
    • Chahine, M.1    Chen, L.Q.2    Fotouhi, N.3    Walsky, R.4    Fry, D.5    Santarelli, V.6    Horn, R.7    Kallen, R.G.8
  • 48
    • 0028055161 scopus 로고
    • A structural model of the tetrodotoxin and saxitoxin binding site of the Na+ channel
    • Lipkind GM, Fozzard HA. A structural model of the tetrodotoxin and saxitoxin binding site of the Na+ channel. Biophys J 1994; 66:1.
    • (1994) Biophys J. , vol.66 , pp. 1
    • Lipkind, G.M.1    Fozzard, H.A.2
  • 49
    • 11244296111 scopus 로고    scopus 로고
    • Modeling P-loops domain of sodium channel: Homology with potassium channels and interaction with ligands
    • Tikhonov DB, Zhorov BS. Modeling P-loops domain of sodium channel: Homology with potassium channels and interaction with ligands. Biophys J 2005; 88:184-97.
    • (2005) Biophys J. , vol.88 , pp. 184-197
    • Tikhonov, D.B.1    Zhorov, B.S.2
  • 50
    • 0037424267 scopus 로고    scopus 로고
    • Molecular basis of isoform-specific m-conotoxin block of cardiac, skeletal muscle, and brain Na+ channels
    • Li RA, Ennis IL, Xue T, Nguyen HM, Tomaselli GF, Goldin AL, Marban E. Molecular basis of isoform-specific m-conotoxin block of cardiac, skeletal muscle, and brain Na+ channels. J Biol Chem 2003; 278:8717-24.
    • (2003) J Biol Chem , vol.278 , pp. 8717-8724
    • Li, R.A.1    Ennis, I.L.2    Xue, T.3    Nguyen, H.M.4    Tomaselli, G.F.5    Goldin, A.L.6    Marban, E.7
  • 51
    • 0037196391 scopus 로고    scopus 로고
    • Charge conversion enables quantification of the proximity between a normally-neutral m-conotoxin (GIIIA) site and the Na+ channel pore
    • Li RA, Sato K, Kodama K, Kohno T, Xue T, Tomaselli GF, Marban E. Charge conversion enables quantification of the proximity between a normally-neutral m-conotoxin (GIIIA) site and the Na+ channel pore. FEBS Lett 2002; 511:159-64.
    • (2002) FEBS Lett , vol.511 , pp. 159-164
    • Li, R.A.1    Sato, K.2    Kodama, K.3    Kohno, T.4    Xue, T.5    Tomaselli, G.F.6    Marban, E.7
  • 52
    • 0035918530 scopus 로고    scopus 로고
    • Latent specificity of molecular recognition in sodium channels engineered to discriminate between two indistinguishable m-conotoxins
    • Li RA, Ennis IL, Tomaselli GF, French RJ, Marban E. Latent specificity of molecular recognition in sodium channels engineered to discriminate between two indistinguishable m-conotoxins. Biochemistry 2001; 40:6002-8.
    • (2001) Biochemistry , vol.40 , pp. 6002-6008
    • Li, R.A.1    Ennis, I.L.2    Tomaselli, G.F.3    French, R.J.4    Marban, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.