메뉴 건너뛰기




Volumn 13, Issue 5, 2004, Pages 1197-1208

Solution structure of Phrixotoxin 1, a specific peptide inhibitor of Kv4 potassium channels from the venom of the theraphosid spider Phrixotrichus auratus

Author keywords

NMR; Phrixotoxin 1; Potassium channel gating modifier; Spider toxin; Structure determination

Indexed keywords

PHRIXOTOXIN 1; POTASSIUM CHANNEL BLOCKING AGENT; SPIDER VENOM; UNCLASSIFIED DRUG; VOLTAGE GATED POTASSIUM CHANNEL;

EID: 1942441447     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03584304     Document Type: Article
Times cited : (46)

References (47)
  • 1
    • 0034489434 scopus 로고    scopus 로고
    • Solution structure of HpTX2, a toxin from Heteropoda venatoria spider that blocks Kv4.2 potassium channel
    • Bernard, C., Legros, C., Ferrat, G., Bischoff, U., Marquardt, A., Pongs, O., and Darbon, H. 2000. Solution structure of HpTX2, a toxin from Heteropoda venatoria spider that blocks Kv4.2 potassium channel. Protein Sci. 9: 2059-2067.
    • (2000) Protein Sci. , vol.9 , pp. 2059-2067
    • Bernard, C.1    Legros, C.2    Ferrat, G.3    Bischoff, U.4    Marquardt, A.5    Pongs, O.6    Darbon, H.7
  • 2
    • 0035980211 scopus 로고    scopus 로고
    • Solution structure of Ptu1, a toxin from the assassin bug Peirates turpis that blocks the voltage-sensitive calcium channel N-type
    • Bernard, C., Corzo, G., Mosbah, A., Nakajima, T., and Darbon, H. 2001. Solution structure of Ptu1, a toxin from the assassin bug Peirates turpis that blocks the voltage-sensitive calcium channel N-type. Biochemistry 40: 12795-12800.
    • (2001) Biochemistry , vol.40 , pp. 12795-12800
    • Bernard, C.1    Corzo, G.2    Mosbah, A.3    Nakajima, T.4    Darbon, H.5
  • 3
    • 0030783712 scopus 로고    scopus 로고
    • Solution structure of maurotoxin, a scorpion toxin from Scorpio maurus, with high affinity for voltage-gated potassium channels
    • Blanc, E., Sabatier, J.M., Kharrat, R., Meunier, S., El Ayeb, M., Van Rietschoten, J., and Darbon, H. 1997. Solution structure of maurotoxin, a scorpion toxin from Scorpio maurus, with high affinity for voltage-gated potassium channels. Proteins 29: 321-333.
    • (1997) Proteins , vol.29 , pp. 321-333
    • Blanc, E.1    Sabatier, J.M.2    Kharrat, R.3    Meunier, S.4    El Ayeb, M.5    Van Rietschoten, J.6    Darbon, H.7
  • 5
    • 0033833498 scopus 로고    scopus 로고
    • Isolation, synthesis and pharmacological characterization of δ-palutoxins IT, novel insecticidal toxins from the spider Paracoelotes luctuosus (Amaurobiidae)
    • Corzo, G., Escoubas, P., Stankiewicz, M., Pelhate, M., Kristensen, C.P., and Nakajima, T. 2000. Isolation, synthesis and pharmacological characterization of δ-palutoxins IT, novel insecticidal toxins from the spider Paracoelotes luctuosus (Amaurobiidae). Eur. J. Biochem. 267: 5783-5795.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5783-5795
    • Corzo, G.1    Escoubas, P.2    Stankiewicz, M.3    Pelhate, M.4    Kristensen, C.P.5    Nakajima, T.6
  • 6
    • 0035239222 scopus 로고    scopus 로고
    • The cystine knot motif in toxins and implications for drug design
    • Craik, D.J., Daly, N.L., and Waine, C. 2001. The cystine knot motif in toxins and implications for drug design. Toxicon 39: 43-60.
    • (2001) Toxicon , vol.39 , pp. 43-60
    • Craik, D.J.1    Daly, N.L.2    Waine, C.3
  • 7
    • 6544276937 scopus 로고    scopus 로고
    • On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures
    • Dauplais, M., Lecoq, A., Song, J., Cotton, J., Jamin, N., Gilquin, B., Roumestand, C., Vita, C., de Medeiros, C.L., Rowan, E.G., et al. 1997. On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures. J. Biol. Chem. 272: 4302-4309.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4302-4309
    • Dauplais, M.1    Lecoq, A.2    Song, J.3    Cotton, J.4    Jamin, N.5    Gilquin, B.6    Roumestand, C.7    Vita, C.8    De Medeiros, C.L.9    Rowan, E.G.10
  • 8
    • 0037382348 scopus 로고    scopus 로고
    • Detergent-assisted oxidative folding of δ-conotoxins
    • DeLa Cruz, R., Buczek, O., Bulaj, G., and Whitby, F.G. 2003. Detergent-assisted oxidative folding of δ-conotoxins. J. Pept. Res. 61: 202-212.
    • (2003) J. Pept. Res. , vol.61 , pp. 202-212
    • DeLa Cruz, R.1    Buczek, O.2    Bulaj, G.3    Whitby, F.G.4
  • 9
    • 0032921154 scopus 로고    scopus 로고
    • Effects of phrixotoxins on the Kv4 family of potassium channels and implications for the role of Ito1 in cardiac electrogenesis
    • Diochot, S., Drici, M.D., Moinier, D., Fink, M., and Lazdunski, M. 1999. Effects of phrixotoxins on the Kv4 family of potassium channels and implications for the role of Ito1 in cardiac electrogenesis. Br. J. Pharmacol. 126: 251-263.
    • (1999) Br. J. Pharmacol. , vol.126 , pp. 251-263
    • Diochot, S.1    Drici, M.D.2    Moinier, D.3    Fink, M.4    Lazdunski, M.5
  • 10
    • 0026193519 scopus 로고
    • Efficient analysis of protein 2D NMR spectra using the software package EASY
    • Eccles, C., Güntert, P., Billeter, M., and Wüthrich, K. 1991. Efficient analysis of protein 2D NMR spectra using the software package EASY. J. Biomol. NMR 1: 111-130.
    • (1991) J. Biomol. NMR , vol.1 , pp. 111-130
    • Eccles, C.1    Güntert, P.2    Billeter, M.3    Wüthrich, K.4
  • 12
    • 0033731951 scopus 로고    scopus 로고
    • Structure and pharmacology of spider venom neurotoxins
    • Escoubas, P., Diochot, S., and Corzo, G. 2000b. Structure and pharmacology of spider venom neurotoxins. Biochimie 82: 893-907.
    • (2000) Biochimie , vol.82 , pp. 893-907
    • Escoubas, P.1    Diochot, S.2    Corzo, G.3
  • 13
    • 0036088553 scopus 로고    scopus 로고
    • Novel tarantula toxins for subtypes of voltage-dependent potassium channels in the Kv2 and Kv4 subfamilies
    • Escoubas, P., Diochot, S., Célérier, M.L., Nakajima, T., and Lazdunski, M. 2002. Novel tarantula toxins for subtypes of voltage-dependent potassium channels in the Kv2 and Kv4 subfamilies. Mol. Pharmacol. 62: 48-57.
    • (2002) Mol. Pharmacol. , vol.62 , pp. 48-57
    • Escoubas, P.1    Diochot, S.2    Célérier, M.L.3    Nakajima, T.4    Lazdunski, M.5
  • 14
    • 0037634059 scopus 로고    scopus 로고
    • Recombinant production and solution structure of PcTx1, the specific peptide inhibitor of ASIC1a proton-gated cation channels
    • Escoubas, P., Bernard, C., Lambeau, G., Lazdunski, M., and Darbon, H. 2003. Recombinant production and solution structure of PcTx1, the specific peptide inhibitor of ASIC1a proton-gated cation channels. Protein Sci. 12: 1332-1343.
    • (2003) Protein Sci. , vol.12 , pp. 1332-1343
    • Escoubas, P.1    Bernard, C.2    Lambeau, G.3    Lazdunski, M.4    Darbon, H.5
  • 17
    • 0026089657 scopus 로고
    • Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA
    • Güntert, P., Braun, W., and Wüthrich, K. 1991. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J. Mol. Biol. 217: 517-530.
    • (1991) J. Mol. Biol. , vol.217 , pp. 517-530
    • Güntert, P.1    Braun, W.2    Wüthrich, K.3
  • 19
    • 0029078447 scopus 로고
    • Solution structure of an Old World-like neurotoxin from the venom of the New World scorpion Centruroides sculpturatus Ewing
    • Jablonsky, M.J., Watt, D.D., and Krishna, N.R. 1995. Solution structure of an Old World-like neurotoxin from the venom of the New World scorpion Centruroides sculpturatus Ewing. J. Mol. Biol. 248: 449-458.
    • (1995) J. Mol. Biol. , vol.248 , pp. 449-458
    • Jablonsky, M.J.1    Watt, D.D.2    Krishna, N.R.3
  • 21
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24: 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 22
    • 0030175309 scopus 로고    scopus 로고
    • Oxidative folding of ω-conotoxin MVIIC: Effects of temperature and salt
    • Kubo, S., Chino, N., Kimura, T., and Sakakibara, S. 1996. Oxidative folding of ω-conotoxin MVIIC: Effects of temperature and salt. Biopolymers 38: 733-744.
    • (1996) Biopolymers , vol.38 , pp. 733-744
    • Kubo, S.1    Chino, N.2    Kimura, T.3    Sakakibara, S.4
  • 23
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R.A., Rullmannn, J.A., MacArthur, M.W., Kaptein, R., and Thornton, J.M. 1996. AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8: 477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 24
    • 0034130607 scopus 로고    scopus 로고
    • Localization and molecular determinants of the Hanatoxin receptors on the voltage-sensing domains of a K(+) channel
    • Li-Smerin, Y. and Swartz, K.J. 2000. Localization and molecular determinants of the Hanatoxin receptors on the voltage-sensing domains of a K(+) channel. J. Gen. Physiol. 115: 673-684.
    • (2000) J. Gen. Physiol. , vol.115 , pp. 673-684
    • Li-Smerin, Y.1    Swartz, K.J.2
  • 25
    • 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
    • -. 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
  • 28
    • 45249127991 scopus 로고
    • Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins
    • Marion, D., Ikura, M., Tschudin, R., and Bax, A. 1989. Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins. J. Magn. Res. 85: 393-399.
    • (1989) J. Magn. Res. , vol.85 , pp. 393-399
    • Marion, D.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 29
    • 0032528988 scopus 로고    scopus 로고
    • Recommendations for the presentation of NMR structures of proteins and nucleic acids-IUPAC-IUBMB-IUPAB Inter-Union Task Group on the standardization of data bases of protein and nucleic acid structures determined by NMR spectroscopy
    • Markley, J.L., Bax, A., Arata, Y., Hilbers, C.W., Kaptein, R., Sykes, B.D., Wright, P.E., and Wüthrich, K. 1998. Recommendations for the presentation of NMR structures of proteins and nucleic acids-IUPAC-IUBMB-IUPAB Inter-Union Task Group on the standardization of data bases of protein and nucleic acid structures determined by NMR spectroscopy. Eur. J. Biochem. 256: 1-15.
    • (1998) Eur. J. Biochem. , vol.256 , pp. 1-15
    • Markley, J.L.1    Bax, A.2    Arata, Y.3    Hilbers, C.W.4    Kaptein, R.5    Sykes, B.D.6    Wright, P.E.7    Wüthrich, K.8
  • 30
    • 0034663625 scopus 로고    scopus 로고
    • A new fold in the scorpion toxin family, associated with an activity on a ryanodine-sensitive calcium channel
    • Mosbah, A., Kharrat, R., Fajloun, Z., Renisio, J.G., Blanc, E., Sabatier, J.M., El Ayeb, M., and Darbon, H. 2000. A new fold in the scorpion toxin family, associated with an activity on a ryanodine-sensitive calcium channel. Proteins 40: 436-442.
    • (2000) Proteins , vol.40 , pp. 436-442
    • Mosbah, A.1    Kharrat, R.2    Fajloun, Z.3    Renisio, J.G.4    Blanc, E.5    Sabatier, J.M.6    El Ayeb, M.7    Darbon, H.8
  • 31
    • 84986486656 scopus 로고
    • A rapid finite difference algorithm, utililizing successive over-relaxation to solve the Poisson-Boltzman equation
    • Nicholls, A. and Honig, B. 1991. A rapid finite difference algorithm, utililizing successive over-relaxation to solve the Poisson-Boltzman equation. J. Comput. Chem. 12: 435-445.
    • (1991) J. Comput. Chem. , vol.12 , pp. 435-445
    • Nicholls, A.1    Honig, B.2
  • 32
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A., and Honig, B. 1991. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11: 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 33
    • 0031796848 scopus 로고    scopus 로고
    • The cystine knot structure of ion channel toxins and related polypeptides
    • Norton, R.S. and Pallaghy, P.K. 1998. The cystine knot structure of ion channel toxins and related polypeptides. Toxicon 36: 1573-1583.
    • (1998) Toxicon , vol.36 , pp. 1573-1583
    • Norton, R.S.1    Pallaghy, P.K.2
  • 34
    • 0029986992 scopus 로고    scopus 로고
    • Three-dimensional structure analysis of μ-agatoxins: Further evidence for common motifs among neurotoxins with diverse ion channel specificities
    • Omecinsky, D.O., Holub, K.E., Adams, M.E., and Reily, M.D. 1996. Three-dimensional structure analysis of μ-agatoxins: Further evidence for common motifs among neurotoxins with diverse ion channel specificities. Biochemistry 35: 2836-2844.
    • (1996) Biochemistry , vol.35 , pp. 2836-2844
    • Omecinsky, D.O.1    Holub, K.E.2    Adams, M.E.3    Reily, M.D.4
  • 35
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V., and Sklenar, V. 1992. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2: 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 39
    • 0032554613 scopus 로고    scopus 로고
    • Three-dimensional structure of κ-conotoxin PVIIA, a novel potassium channel-blocking toxin from cone snails
    • Savarin, P., Guenneugues, M., Gilquin, B., Lamthanh, H., Gasparini, S., Zinn-Justin, S., and Ménez, A. 1998. Three-dimensional structure of κ-conotoxin PVIIA, a novel potassium channel-blocking toxin from cone snails. Biochemistry 37: 5407-5416.
    • (1998) Biochemistry , vol.37 , pp. 5407-5416
    • Savarin, P.1    Guenneugues, M.2    Gilquin, B.3    Lamthanh, H.4    Gasparini, S.5    Zinn-Justin, S.6    Ménez, A.7
  • 40
    • 0031574335 scopus 로고    scopus 로고
    • Solution structure and proposed binding mechanism of a novel potassium channel toxin κ-conotoxin PVIIA
    • Scanlon, M.J., Naranjo, D., Thomas, L., Alewood, P.F., Lewis, R.J., and Craik, D.J. 1997. Solution structure and proposed binding mechanism of a novel potassium channel toxin κ-conotoxin PVIIA. Structure 5: 1585-1597.
    • (1997) Structure , vol.5 , pp. 1585-1597
    • Scanlon, M.J.1    Naranjo, D.2    Thomas, L.3    Alewood, P.F.4    Lewis, R.J.5    Craik, D.J.6
  • 41
    • 0142232008 scopus 로고    scopus 로고
    • Structural basis of binding and inhibition of novel tarantula toxins in mammalian voltage-dependent potassium channels
    • Shiau, Y.S., Huang, P.T., Liou, H.H., Liaw, Y.C, Shiau, Y.Y., and Lou, K.L. 2003. Structural basis of binding and inhibition of novel tarantula toxins in mammalian voltage-dependent potassium channels. Chem. Res. Toxicol. 16: 1217-1225.
    • (2003) Chem. Res. Toxicol. , vol.16 , pp. 1217-1225
    • Shiau, Y.S.1    Huang, P.T.2    Liou, H.H.3    Liaw, Y.C.4    Shiau, Y.Y.5    Lou, K.L.6
  • 43
    • 0028811258 scopus 로고
    • An inhibitor of the Kv2.1 potassium channel isolated from the venom of a Chilean tarantula
    • Swartz, K.J. and MacKinnon, R. 1995. An inhibitor of the Kv2.1 potassium channel isolated from the venom of a Chilean tarantula. Neuron 15: 941-949.
    • (1995) Neuron , vol.15 , pp. 941-949
    • Swartz, K.J.1    MacKinnon, R.2
  • 44
    • 0030952979 scopus 로고    scopus 로고
    • + channel through multiple binding sites
    • + channel through multiple binding sites. Neuron 18: 665-673.
    • (1997) Neuron , vol.18 , pp. 665-673
  • 45
    • 0030935699 scopus 로고    scopus 로고
    • + channels
    • + channels. Neuron 18: 675-682.
    • (1997) Neuron , vol.18 , pp. 675-682
  • 46
    • 0034737306 scopus 로고    scopus 로고
    • Solution structure of hanatoxin1, a gating modifier of voltage-dependent K(+) channels: Common surface features of gating modifier toxins
    • Takahashi, H., Kim, J.I., Min, H.J., Sato, K., Swartz, K.J., and Shimada, I. 2000. Solution structure of hanatoxin1, a gating modifier of voltage-dependent K(+) channels: Common surface features of gating modifier toxins. J. Mol. Biol. 297: 771-780.
    • (2000) J. Mol. Biol. , vol.297 , pp. 771-780
    • Takahashi, H.1    Kim, J.I.2    Min, H.J.3    Sato, K.4    Swartz, K.J.5    Shimada, I.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.