메뉴 건너뛰기




Volumn 47, Issue 3, 2008, Pages 911-921

NMR analysis of interaction of LqhαIT scorpion toxin with a peptide corresponding to the D4/S3-S4 loop of insect para voltage-gated sodium channel

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELL CULTURE; ELECTRIC EXCITATION; MOLECULAR INTERACTIONS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

EID: 38549142601     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701323k     Document Type: Article
Times cited : (18)

References (52)
  • 1
    • 0033694833 scopus 로고    scopus 로고
    • From ionic currents to molecular mechanisms: The structure and function of voltage-gated sodium channels
    • Catterall, W. A. (2000) From ionic currents to molecular mechanisms: The structure and function of voltage-gated sodium channels, Neuron 26, 13-25.
    • (2000) Neuron , vol.26 , pp. 13-25
    • Catterall, W.A.1
  • 2
    • 0033731909 scopus 로고    scopus 로고
    • Molecular mechanisms of neurotoxin action on voltage-gated sodium channels
    • Cestele, S., and Catterall, W. A. (2000) Molecular mechanisms of neurotoxin action on voltage-gated sodium channels, Biochimie 82, 883-892.
    • (2000) Biochimie , vol.82 , pp. 883-892
    • Cestele, S.1    Catterall, W.A.2
  • 4
    • 0035931872 scopus 로고    scopus 로고
    • A 3D view of sodium channels
    • Catterall, W. A. (2001) A 3D view of sodium channels, Nature 409, 988-991.
    • (2001) Nature , vol.409 , pp. 988-991
    • Catterall, W.A.1
  • 6
    • 33751229668 scopus 로고    scopus 로고
    • Roles of voltage-dependent sodium channels in neuronal development, pain, and neurodegeneration
    • Wada, A. (2006) Roles of voltage-dependent sodium channels in neuronal development, pain, and neurodegeneration, J. Pharmacol. Sci. 102, 253-268.
    • (2006) J. Pharmacol. Sci , vol.102 , pp. 253-268
    • Wada, A.1
  • 10
    • 0030021584 scopus 로고    scopus 로고
    • Molecular basis of charge movement in voltage-gated sodium channels
    • Yang, N., George, A. L., Jr., and Horn, R. (1996) Molecular basis of charge movement in voltage-gated sodium channels, Neuron 16, 113-122.
    • (1996) Neuron , vol.16 , pp. 113-122
    • Yang, N.1    George Jr., A.L.2    Horn, R.3
  • 11
    • 0032805568 scopus 로고    scopus 로고
    • The Na channel voltage sensor associated with inactivation is localized to the external charged residues of domain IV, S4
    • Sheets, M. F., Kyle, J. W., Kallen, R. G., and Hanck, D. A. (1999) The Na channel voltage sensor associated with inactivation is localized to the external charged residues of domain IV, S4, Biophys. J. 77, 747-757.
    • (1999) Biophys. J , vol.77 , pp. 747-757
    • Sheets, M.F.1    Kyle, J.W.2    Kallen, R.G.3    Hanck, D.A.4
  • 13
    • 0037290637 scopus 로고    scopus 로고
    • Voltage-gated sodium channels as primary targets of diverse lipid-soluble neurotoxins
    • Wang, S. Y., and Wang, G. K. (2003) Voltage-gated sodium channels as primary targets of diverse lipid-soluble neurotoxins, Cell. Signalling 15, 151-159.
    • (2003) Cell. Signalling , vol.15 , pp. 151-159
    • Wang, S.Y.1    Wang, G.K.2
  • 14
    • 0036897456 scopus 로고    scopus 로고
    • The sea anemone toxins BgII and BgIII prolong the inactivation time course of the tetrodotoxin- sensitive sodium current in rat dorsal root ganglion neurons
    • Salceda, E., Garateix, A., and Soto, E. (2002) The sea anemone toxins BgII and BgIII prolong the inactivation time course of the tetrodotoxin- sensitive sodium current in rat dorsal root ganglion neurons, J. Pharmacol. Exp. Ther. 303, 1067-1074.
    • (2002) J. Pharmacol. Exp. Ther , vol.303 , pp. 1067-1074
    • Salceda, E.1    Garateix, A.2    Soto, E.3
  • 15
    • 0030009637 scopus 로고    scopus 로고
    • Scorpion toxins affecting sodium current inactivation bind to distinct homologous receptor sites on rat brain and insect sodium channels
    • Gordon, D., Martin-Eauclaire, M. F., Cestele, S., Kopeyan, C., Carlier, E., Khalifa, R. B., Pelhate, M., and Rochat, H. (1996) Scorpion toxins affecting sodium current inactivation bind to distinct homologous receptor sites on rat brain and insect sodium channels, J. Biol. Chem. 271, 8034-8045.
    • (1996) J. Biol. Chem , vol.271 , pp. 8034-8045
    • Gordon, D.1    Martin-Eauclaire, M.F.2    Cestele, S.3    Kopeyan, C.4    Carlier, E.5    Khalifa, R.B.6    Pelhate, M.7    Rochat, H.8
  • 16
    • 0024240855 scopus 로고
    • Site of covalent attachment of α-scorpion toxin derivatives in domain I of the sodium channel α subunit
    • Tejedor, F. J., and Catterall, W. A. (1988) Site of covalent attachment of α-scorpion toxin derivatives in domain I of the sodium channel α subunit, Proc. Natl. Acad. Sci. U.S.A. 85, 8742-8746.
    • (1988) Proc. Natl. Acad. Sci. U.S.A , vol.85 , pp. 8742-8746
    • Tejedor, F.J.1    Catterall, W.A.2
  • 17
    • 0024811112 scopus 로고
    • Localization of the receptor site for α-scorpion toxins by antibody mapping: Implications for sodium channel topology
    • Thomsen, W. J., and Catterall, W. A. (1989) Localization of the receptor site for α-scorpion toxins by antibody mapping: Implications for sodium channel topology, Proc. Natl. Acad. Sci. U.S.A. 86, 10161-10165.
    • (1989) Proc. Natl. Acad. Sci. U.S.A , vol.86 , pp. 10161-10165
    • Thomsen, W.J.1    Catterall, W.A.2
  • 18
    • 33746369777 scopus 로고    scopus 로고
    • Structure and function of the voltage sensor of sodium channels probed by a β-scorpion toxin
    • Cestele, S., Yarov-Yarovoy, V., Qu, Y., Sampieri, F., Scheuer, T., and Catterall, W. A. (2006) Structure and function of the voltage sensor of sodium channels probed by a β-scorpion toxin, J. Biol. Chem. 281, 21332-21344.
    • (2006) J. Biol. Chem , vol.281 , pp. 21332-21344
    • Cestele, S.1    Yarov-Yarovoy, V.2    Qu, Y.3    Sampieri, F.4    Scheuer, T.5    Catterall, W.A.6
  • 19
    • 21744442274 scopus 로고    scopus 로고
    • Genetic polymorphism and expression of a highly potent scorpion depressant toxin enable refinement of the effects on insect Na channels and illuminate the key role of Asn-58
    • Strugatsky, D., Zilberberg, N., Stankiewicz, M., Ilan, N., Turkov, M., Cohen, L., Pelhate, M., Gilles, N., Gordon, D., and Gurevitz, M. (2005) Genetic polymorphism and expression of a highly potent scorpion depressant toxin enable refinement of the effects on insect Na channels and illuminate the key role of Asn-58, Biochemistry 44, 9179-9187.
    • (2005) Biochemistry , vol.44 , pp. 9179-9187
    • Strugatsky, D.1    Zilberberg, N.2    Stankiewicz, M.3    Ilan, N.4    Turkov, M.5    Cohen, L.6    Pelhate, M.7    Gilles, N.8    Gordon, D.9    Gurevitz, M.10
  • 22
    • 1342287128 scopus 로고    scopus 로고
    • Combinatorial interaction of scorpion toxins Lqh-2, Lqh-3, and LqhαIT with sodium channel receptor sites-3
    • Leipold, E., Lu, S., Gordon, D., Hansel, A., and Heinemann, S. H. (2004) Combinatorial interaction of scorpion toxins Lqh-2, Lqh-3, and LqhαIT with sodium channel receptor sites-3, Mol. Pharmacol. 65, 685-691.
    • (2004) Mol. Pharmacol , vol.65 , pp. 685-691
    • Leipold, E.1    Lu, S.2    Gordon, D.3    Hansel, A.4    Heinemann, S.H.5
  • 23
    • 0037306968 scopus 로고    scopus 로고
    • The selectivity of scorpion α-toxins for sodium channel subtypes is determined by subtle variations at the interacting surface
    • Gordon, D., and Gurevitz, M. (2003) The selectivity of scorpion α-toxins for sodium channel subtypes is determined by subtle variations at the interacting surface, Toxicon 41, 125-128.
    • (2003) Toxicon , vol.41 , pp. 125-128
    • Gordon, D.1    Gurevitz, M.2
  • 24
    • 33847400659 scopus 로고    scopus 로고
    • Sodium channel features that confer differential sensitivity to various scorpion α-toxins
    • Beadle, D. J, Mellor, I. R, and Usherwood, P. N. R, Eds, Society of Chemical Industry, London
    • Gordon, D., Kallen, R. G., and Heinemann, S. H. (2004) Sodium channel features that confer differential sensitivity to various scorpion α-toxins, in Neurotox '03: Neurotoxicological Targets from Functional Genomics and Proteomics (Beadle, D. J., Mellor, I. R., and Usherwood, P. N. R., Eds.) Society of Chemical Industry, London.
    • (2004) Neurotox '03: Neurotoxicological Targets from Functional Genomics and Proteomics
    • Gordon, D.1    Kallen, R.G.2    Heinemann, S.H.3
  • 25
    • 33847366129 scopus 로고    scopus 로고
    • The differential preference of scorpion α-toxins for insect or mammalian sodium channels: Implications for improved insect control
    • Gordon, D., Karbat, I., Ilan, N., Cohen, L., Kahn, R., Gilles, N., Dong, K., Stuhmer, W., Tytgat, J., and Gurevitz, M. (2007) The differential preference of scorpion α-toxins for insect or mammalian sodium channels: Implications for improved insect control, Toxicon 49, 452-472.
    • (2007) Toxicon , vol.49 , pp. 452-472
    • Gordon, D.1    Karbat, I.2    Ilan, N.3    Cohen, L.4    Kahn, R.5    Gilles, N.6    Dong, K.7    Stuhmer, W.8    Tytgat, J.9    Gurevitz, M.10
  • 26
    • 0025303099 scopus 로고
    • A scorpion venom neurotoxin paralytic to insects that affects sodium current inactivation: Purification, primary structure, and mode of action
    • Eitan, M., Fowler, E., Herrmann, R., Duval, A., Pelhate, M., and Zlotkin, E. (1990) A scorpion venom neurotoxin paralytic to insects that affects sodium current inactivation: Purification, primary structure, and mode of action, Biochemistry 29, 5941-5947.
    • (1990) Biochemistry , vol.29 , pp. 5941-5947
    • Eitan, M.1    Fowler, E.2    Herrmann, R.3    Duval, A.4    Pelhate, M.5    Zlotkin, E.6
  • 27
    • 0031017788 scopus 로고    scopus 로고
    • Solution structures of a highly insecticidal recombinant scorpion α-toxin and a mutant with increased activity
    • Tugarinov, V., Kustanovich, I., Zilberberg, N., Gurevitz, M., and Anglister, J. (1997) Solution structures of a highly insecticidal recombinant scorpion α-toxin and a mutant with increased activity, Biochemistry 36, 2414-2424.
    • (1997) Biochemistry , vol.36 , pp. 2414-2424
    • Tugarinov, V.1    Kustanovich, I.2    Zilberberg, N.3    Gurevitz, M.4    Anglister, J.5
  • 28
    • 0030951334 scopus 로고    scopus 로고
    • Identification of structural elements of a scorpion α-neurotoxin important for receptor site recognition
    • Zilberberg, N., Froy, O., Loret, E., Cestele, S., Arad, D., Gordon, D., and Gurevitz, M. (1997) Identification of structural elements of a scorpion α-neurotoxin important for receptor site recognition, J. Biol. Chem. 272, 14810-14816.
    • (1997) J. Biol. Chem , vol.272 , pp. 14810-14816
    • Zilberberg, N.1    Froy, O.2    Loret, E.3    Cestele, S.4    Arad, D.5    Gordon, D.6    Gurevitz, M.7
  • 30
    • 21844466444 scopus 로고    scopus 로고
    • Molecular interaction of δ-conotoxins with voltage-gated sodium channels
    • Leipold, E., Hansel, A., Olivera, B. M., Terlau, H., and Heinemann, S. H. (2005) Molecular interaction of δ-conotoxins with voltage-gated sodium channels, FEBS Lett. 579, 3881-3884.
    • (2005) FEBS Lett , vol.579 , pp. 3881-3884
    • Leipold, E.1    Hansel, A.2    Olivera, B.M.3    Terlau, H.4    Heinemann, S.H.5
  • 32
    • 0035931906 scopus 로고    scopus 로고
    • The voltage-sensitive sodium channel is a bell-shaped molecule with several cavities
    • Sato, C., Ueno, Y., Asai, K., Takahashi, K., Sato, M., Engel, A., and Fujiyoshi, Y. (2001) The voltage-sensitive sodium channel is a bell-shaped molecule with several cavities, Nature 409, 1047-1051.
    • (2001) Nature , vol.409 , pp. 1047-1051
    • Sato, C.1    Ueno, Y.2    Asai, K.3    Takahashi, K.4    Sato, M.5    Engel, A.6    Fujiyoshi, Y.7
  • 33
    • 0027371744 scopus 로고
    • NMR solution structure of an α-bungarotoxin/nicotinic receptor peptide complex
    • Basus, V. J., Song, G., and Hawrot, E. (1993) NMR solution structure of an α-bungarotoxin/nicotinic receptor peptide complex, Biochemistry 32, 12290-12298.
    • (1993) Biochemistry , vol.32 , pp. 12290-12298
    • Basus, V.J.1    Song, G.2    Hawrot, E.3
  • 34
    • 0037130458 scopus 로고    scopus 로고
    • The mechanism for acetylcholine receptor inhibition by α-neurotoxins and species-specific resistance to α-bungarotoxin revealed by NMR
    • Samson, A., Scherf, T., Eisenstein, M., Chill, J., and Anglister, J. (2002) The mechanism for acetylcholine receptor inhibition by α-neurotoxins and species-specific resistance to α-bungarotoxin revealed by NMR, Neuron 35, 319-332.
    • (2002) Neuron , vol.35 , pp. 319-332
    • Samson, A.1    Scherf, T.2    Eisenstein, M.3    Chill, J.4    Anglister, J.5
  • 35
    • 0026770069 scopus 로고
    • Induced peptide conformations in different antibody complexes: Molecular modeling of the three-dimensional structure of peptide-antibody complexes using NMR-derived distance restraints
    • Scherf, T., Hiller, R., Naider, F., Levitt, M., and Anglister, J. (1992) Induced peptide conformations in different antibody complexes: Molecular modeling of the three-dimensional structure of peptide-antibody complexes using NMR-derived distance restraints, Biochemistry 31, 6884-6897.
    • (1992) Biochemistry , vol.31 , pp. 6884-6897
    • Scherf, T.1    Hiller, R.2    Naider, F.3    Levitt, M.4    Anglister, J.5
  • 37
    • 0017637022 scopus 로고
    • Cleavage at Asn-Gly bonds with hydroxylamine
    • Bornstein, P., and Balian, G. (1977) Cleavage at Asn-Gly bonds with hydroxylamine, Methods Enzymol. 47, 132-145.
    • (1977) Methods Enzymol , vol.47 , pp. 132-145
    • Bornstein, P.1    Balian, G.2
  • 38
    • 0035023528 scopus 로고    scopus 로고
    • Helical structure of the COOH terminus of S3 and its contribution to the gating modifier toxin receptor in voltage-gated ion channels
    • Li-Smerin, Y., and Swartz, K. J. (2001) Helical structure of the COOH terminus of S3 and its contribution to the gating modifier toxin receptor in voltage-gated ion channels, J. Gen. Physiol. 117, 205-218.
    • (2001) J. Gen. Physiol , vol.117 , pp. 205-218
    • Li-Smerin, Y.1    Swartz, K.J.2
  • 39
    • 0036715180 scopus 로고    scopus 로고
    • Movement and crevices around a sodium channel S3 segment
    • Nguyen, T. P., and Horn, R. (2002) Movement and crevices around a sodium channel S3 segment, J. Gen. Physiol. 120, 419-436.
    • (2002) J. Gen. Physiol , vol.120 , pp. 419-436
    • Nguyen, T.P.1    Horn, R.2
  • 41
    • 0036618134 scopus 로고    scopus 로고
    • Domain 2 of Drosophila para voltage-gated sodium channel confers insect properties to a rat brain channel
    • Shichor, I., Zlotkin, E., Ilan, N., Chikashvili, D., Stuhmer, W., Gordon, D., and Lotan, I. (2002) Domain 2 of Drosophila para voltage-gated sodium channel confers insect properties to a rat brain channel, J. Neurosci. 22, 4364-4371.
    • (2002) J. Neurosci , vol.22 , pp. 4364-4371
    • Shichor, I.1    Zlotkin, E.2    Ilan, N.3    Chikashvili, D.4    Stuhmer, W.5    Gordon, D.6    Lotan, I.7
  • 42
    • 33746220061 scopus 로고    scopus 로고
    • Expression and mutagenesis of the sea anemone toxin Av2 reveals key amino acid residues important for activity on voltage-gated sodium channels
    • Moran, Y., Cohen, L., Kahn, R., Karbat, I., Gordon, D., and Gurevitz, M. (2006) Expression and mutagenesis of the sea anemone toxin Av2 reveals key amino acid residues important for activity on voltage-gated sodium channels, Biochemistry 45, 8864-8873.
    • (2006) Biochemistry , vol.45 , pp. 8864-8873
    • Moran, Y.1    Cohen, L.2    Kahn, R.3    Karbat, I.4    Gordon, D.5    Gurevitz, M.6
  • 43
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes, J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 44
    • 34249765651 scopus 로고
    • NMR View: A Computer-Program for the Visualization and Analysis of NMR Data
    • Johnson, B. A., and Blevins, R. A. (1994) NMR View: A Computer-Program for the Visualization and Analysis of NMR Data, J. Biomol. NMR 4, 603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 45
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • Johnson, B. A. (2004) Using NMRView to visualize and analyze the NMR spectra of macromolecules, Methods Mol. Biol. 278, 313-352.
    • (2004) Methods Mol. Biol , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 46
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Shuker, S. B., Hajduk, P. J., Meadows, R. P., and Fesik, S. W. (1996) Discovering high-affinity ligands for proteins: SAR by NMR, Science 274, 1531-1534.
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 47
    • 0037039335 scopus 로고    scopus 로고
    • Mapping protein-protein interactions in solution by NMR spectroscopy
    • Zuiderweg, E. R. (2002) Mapping protein-protein interactions in solution by NMR spectroscopy, Biochemistry 41, 1-7.
    • (2002) Biochemistry , vol.41 , pp. 1-7
    • Zuiderweg, E.R.1
  • 49
    • 0033812147 scopus 로고    scopus 로고
    • Structural implications on the interaction of scorpion α-like toxins with the sodium channel receptor site inferred from toxin iodination and pH-dependent binding
    • Gilles, N., Krimm, I., Bouet, F., Froy, O., Gurevitz, M., Lancelin, J. M., and Gordon, D. (2000) Structural implications on the interaction of scorpion α-like toxins with the sodium channel receptor site inferred from toxin iodination and pH-dependent binding, J. Neurochem. 75, 1735-1745.
    • (2000) J. Neurochem , vol.75 , pp. 1735-1745
    • Gilles, N.1    Krimm, I.2    Bouet, F.3    Froy, O.4    Gurevitz, M.5    Lancelin, J.M.6    Gordon, D.7
  • 50
    • 0035011099 scopus 로고    scopus 로고
    • Diversification of neurotoxins by C-tail 'wiggling': A scorpion recipe for survival
    • Gurevitz, M., Gordon, D., Ben-Natan, S., Turkov, M., and Froy, O. (2001) Diversification of neurotoxins by C-tail 'wiggling': A scorpion recipe for survival, FASEB J. 15, 1201-1205.
    • (2001) FASEB J , vol.15 , pp. 1201-1205
    • Gurevitz, M.1    Gordon, D.2    Ben-Natan, S.3    Turkov, M.4    Froy, O.5
  • 51
    • 10044240717 scopus 로고    scopus 로고
    • Mapping the binding of the N-terminal extracellular tail of the CXCR4 receptor to stromal cell-derived factor-1α
    • Gozansky, E. K., Louis, J. M., Caffrey, M., and Clore, G. M. (2005) Mapping the binding of the N-terminal extracellular tail of the CXCR4 receptor to stromal cell-derived factor-1α, J. Mol. Biol. 345, 651-658.
    • (2005) J. Mol. Biol , vol.345 , pp. 651-658
    • Gozansky, E.K.1    Louis, J.M.2    Caffrey, M.3    Clore, G.M.4
  • 52
    • 33845767989 scopus 로고    scopus 로고
    • Recognition of RANTES by extracellular parts of the CCR5 receptor
    • Duma, L., Haussinger, D., Rogowski, M., Lusso, P., and Grzesiek, S. (2007) Recognition of RANTES by extracellular parts of the CCR5 receptor, J. Mol. Biol. 365, 1063-1075.
    • (2007) J. Mol. Biol , vol.365 , pp. 1063-1075
    • Duma, L.1    Haussinger, D.2    Rogowski, M.3    Lusso, P.4    Grzesiek, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.