Solution structure of IsTX: A male scorpion toxin from Opisthacanthus madagascariensis (Ischnuridae)

European Journal of Biochemistry

Volumn 271, Issue 19, 2004, Pages 3855-3864

  Yamaji, Nahoko ^a   Dai, Li ^a   Sugase, Kenji ^a   Andriantsiferana, Marta ^b   Nakajima, Terumi ^a   Iwashita, Takashi ^a  

^a SUNTORY INSTITUTE FOR BIOORGANIC RESEARCH   (Japan)

^b UNIVERSITY OF ANTANANARIVO   (Madagascar)

Author keywords

Cysteine stabilized fold; NMR; Potassium channels; Scorpion toxin; Sex specific toxin

Indexed keywords

ALPHA KTX6 TOXIN; APAMIN; CALCIUM ACTIVATED POTASSIUM CHANNEL; CYSTEINE; HSTX1 TOXIN; ISTX TOXIN; LYSINE; POTASSIUM CHANNEL; POTASSIUM CHANNEL BLOCKING AGENT; POTASSIUM CHANNEL KV1.3; SCORPION VENOM; UNCLASSIFIED DRUG; VOLTAGE GATED POTASSIUM CHANNEL;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; BETA CHAIN; DISULFIDE BOND; ELECTRICITY; HETEROMETRUS SPINIFER; MALE; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; OPISTHACANTHUS MADAGASCARIENSIS; PRIORITY JOURNAL; PROTEIN STABILITY; SCORPION; SEX DIFFERENCE; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CLONING, MOLECULAR; FEMALE; KV1.3 POTASSIUM CHANNEL; MAGNETIC RESONANCE SPECTROSCOPY; MALE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; POTASSIUM CHANNEL BLOCKERS; POTASSIUM CHANNELS, VOLTAGE-GATED; SCORPION VENOMS; SCORPIONS; SEQUENCE HOMOLOGY, AMINO ACID; SEX FACTORS; SOLUTIONS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; STRUCTURE-ACTIVITY RELATIONSHIP; TOXINS, BIOLOGICAL;

HETEROMETRUS; HETEROMETRUS SPINIFER; INVERTEBRATA; LIOCHELIDAE; OPISTHACANTHUS MADAGASCARIENSIS; SCORPIONES;

EID: 4944255599     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04322.x     Document Type: Article

References (53)

1. + channel. J. Biol. Chem. 261, 14607-14613.
2. Park, C.-S. & Miller, C. (1992) Mapping function to structure in a channel-blocking peptide: electrostatic mutants of charybdotoxin. Biochemistry 31, 7749-7755.
3. + channel structure from a complete functional map of the molecular surface of charybdotoxin. Biochemistry 33, 443-450.
4. Blanc, E., Romi-Lebrun, R., Bornet, O., Nakajima, T. & Darbon, H. (1998) Solution structure of two new toxins from the venom of the chinese scorpion Buthus martensi karsch blockers of the potassium channels. Biochemistry 37, 12412-12418.
5. Dai, L., Yasuda, A., Naoki, H., Corzo, G., Andriantsiferana, M. & Nakajima, T. (2001) IsCT, a novel cytotoxic linear peptide from scorpion Opisthacanthus madagascariensis. Biochem. Biophys. Res. Commun. 286, 820-825.
6. Dai, L., Corzo, G., Naoki, H., Andriantsiferana, M. & Nakajima, T. (2002) Purification, structure-function analysis, and molecular characterization of novel linear peptides from scorpion Opisthacanthus madagascariensis. Biochem. Biophys. Res. Commun. 293, 1514-1522.
7. Alewood, D., Birinyi-Strachan, L.C., Pallaghy, P.K., Norton, R.S., Nicholson, G.M. & Alewood, P.F. (2003) Synthesis and characterization of δ-atracotoxin-Ar1a, the lethal neurotoxin from venom of the Sydney funnel-web spider (Atrax robustus). Biochemistry 42, 12933-12940.
8. Gunning, S.J., Chong, Y., Khalife, A.A., Hains, P.G., Broady, K.W. & Nicholson, G.M. (2003) Isolation of delta-missulenatoxin-Mb1a, the major vertebrate-active spider delta-toxin from the venom of Missulena bradleyi (Actinopodidae). FEBS Lett. 554, 211-218.
9. Tytgat, J., George Chandy, K., Garcia, M.L., Gutman, G.A., Martin-Eauclaire, M.-F., van der Walt, J.J. & Possani, L.D. (1999) A unified nomenclature for short-chain peptides isolated from scorpion venoms: α-KTx molecular subfamilies. Trends Pharmacol. Sci. 20, 444-447.
10. + channels and scorpion toxins. Trends Pharmacol. Sci. 24, 222-227.
11. Kharrat, R., Mansuelle, P., Sampieri, F., Crest, M., Oughideni, R., Van Rietschoten, J., Martin-Eauclaire, M.-F., Rochat, H. & El Ayeb, M. (1997) Maurotoxin, a four disulfide bridge toxin from Scorpio maurus venom: purification, structure and action on potassium channels. FEBS Lett. 406, 284-290.
12. Blanc, E., Sabatier, J.-M., Kharrat, R., Meunier, S., El Ayeb, M., Van Rietschoten, J. & 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.
13. Fajloun, Z., Mosbah, A., Carlier, E., Mansuelle, P., Sandoz, G., Fathallah, M., di Luccio, E., Devaux, C., Rochat, H., Darbon, H., De Waard, M. & Sabatier, J.M. (2000) Maurotoxin versus Pi1/HsTX1 toxins: toward new insights in the understanding of their distinct disulfide bridge patterns. J. Biol. Chem. 275, 39394-39402.
14. + channels, isolated from Heterometrus spinnifer (Scorpionidae) venom. Biochem. J. 328, 321-327.
15. Savarin, P., Romi-Lebrun, R., Zinn-Justin, S., Lebrun, B., Nakajima, T., Gilquin, B. & Menez, A. (1999) Structural and functional consequences of the presence of a fourth disulfide bridge in the scorpion short toxins: Solution structure of the potassium channel inhibitor HsTX1. Protein Sci. 8, 2672-2685.
16. Savarin, P., Zinn-Justin, S. & Gilquin, B. (2001) Variability in automated assignment of NOESY spectra and three-dimensional structure determination: a test case on three small disulfide-bonded proteins. J. Biomol. NMR 19, 49-62.
17. 1H NMR analysis using a nano-NMR probe. Biochemistry 36, 2649-2658.
18. Tenenholz, T.C., Rogowski, R.S., Collins, J.H., Blaustein, M.P. & Weber, D.J. (1997) Solution structure for Pandinus toxin K-α (PiTX-Kα), a selective blocker of A-type potassium channels. Biochemistry 36, 2763-2771.
19. 1H-NMR analysis using a nano-NMR probe. Biochemistry 38, 16756-16765.
20. Guijarro, J.I., M'Barek, S., Gomez-Lagunas, F., Garnier, D., Rochat, H., Sabatier, J.-M., Possani, L.D. & Delepierre, M. (2003) Solution structure of Pi4, a short four-disulfide-bridged scorpion toxin specific of potassium channels. Prot. Sci. 12, 1844-1854.
21. Katsumi, A., Tuley, E.A., Bodó, I. & Sadler, J.E. (2000) Localization of disulfide bonds in the cystine knot domain of human von Willebrand Factor. J. Biol. Chem. 275, 25585-25594.
22. 1H NMR spectra of proteins via double quantum filtering. Biochem. Biophys. Res. Commun. 117, 479-485.
23. Kumar, A., Ernst, R.R. & Wüthrich, K. (1980) 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. 95, 1-6.
24. Bodenhausen, G., Kogler, H. & Ernst, R.R. (1984) Selection of coherence-transfer pathways in NMR pulse experiments. J. Magn. Reson. 58, 370-388.
25. Bax, A. & Davis, D.G. (1985) MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65, 355-360.
26. Piotto, M., Saudek, V. & Sklenar, V. (1992) Gradient-tailored excitation for single quantum spectroscopy of aqueous solutions. J. Biomol. NMR 2, 661-665.
27. Palmer, A.G., Cavanagh, J., Wright, P.E. & Rance, M. (1991) Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy. J. Magn. Reson. 93, 151-170.
28. Kay, L.E., Keifer, P. & Saarinen, T. (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114, 10663-10665.
29. Wüthrich, K. (1986) NMR of Protein and Nucleic Acids. John Wiley & Sons, Inc, New York.
30. H 2D NMR spectra by interactive computer graphics. J. Magn. Reson. 84, 627-633.
31. Andersen, N.H., Neidigh, J.W., Harris, S.M., Lee, G.M., Liu, Z. & Tong, H. (1997) Extracting information from the temperature gradients of polypeptide NH chemical shifts. 1. The importance of conformational averaging. J. Am. Chem. Soc. 119, 8547-8561.
32. Cierpicki, T., Zhoukov, I., Byrd, R.A. & Otlewski, J. (2002) Hydrogen bonds in human ubiquitin reflected in temperature coefficients of amide protons. J. Magn. Reson. 157, 178-180.
33. HNα for identification of helical secondary structure. J. Mol. Biol. 180, 741-751.
34. Clore, G.M. & Gronenborn, A.M. (1998) New methods of structure refinement for macromolecular structure determination by NMR. Proc. Natl Acad. Sci. USA 95, 5891-5898.
35. Schwieters, C.D., Kuszewski, J.J., Tjandra, N. & Clore, G.M. (2003) The Xplor-NIH NMR molecular structure determination package. J. Magn. Reson. 160, 66-74.
36. Brunger, A.T. (1992) X-PLOR, Version 3.1 Manual. Yale University Press, New Haven, CT, USA.
37. Lakowski, R.A., Rullmann, J.A., MacArthur, M.W., Kaptein, R. & 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.
38. 13C nuclear magnetic resonance chemical shifts. J. Am. Chem. Soc. 113, 5490-5492.
39. β chemical shifts on protein structure determination by NMR. J. Magn. Reson. Series B 106, 92-96.
40. Cierpicki, T. & Otlewski, J. (2000) Determination of a high precision structure of a novel protein, Linum usitatissimum trypsin inhibitor (LUTI), using computer-aided assignment of NOESY. J. Mol. Biol. 302, 1179-1192.
41. Koradi, R., Billeter, M. & Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55.
42. + channels. Eur. J. Biochem. 242, 491-498.
43. Kharrat, R., Mansuelle, P., Sampieri, F., Crest, M., Oughideni, R., Van Rietschoten, J., Martin-Eauclair, M.-F., Rochat, H. & El Ayeb, M. (1997) Maurotoxin, a four disulfide bridge toxin from Scorpio maurus venom: purification, structure and action o potassium channels. FEBS Lett. 406, 284-290.
44. + channels by Pi1, a novel class of scorpion toxin. FEBS Lett. 400, 197-200.
45. + channels. Eur. J. Biochem. 267, 5149-5155.
46. + channel. Nature 423, 33-41.
47. + channel. Nature 423, 42-48.
48. Mackinnon, R., Cohen, S.L., Kuo, A., Lee, A. & Chait, B.T. (1998) Structural conservation in prokaryotic and eukaryotic potassium channels. Science 280, 106-109.
49. Fu, W., Cui, M., Briggs, J.M., Huang, X., Xiong, B., Zhang, Y., Luo, X., Shen, J., Ji, R., Jiang, H. & Chen, K. (2002) Brownian dynamics simulations of the recognition of the scorpion toxin maurotoxin with the voltage-gated potassium ion channels. Biophys. J. 83, 2370-2385.
50. Zhang, M., Korolkova, Y.V., Liu, J., Jiang, M., Grishin, E.V. & Tseng, G.-N. (2003) BeKm-1 is a HERG-specific toxin that shares the structure with ChTx but the mechanism of action with ErgTx1. Biopys. J. 84, 3022-3036.
51. + channels. Eur. J. Biochem. 270, 3583-3592.
52. + channel from squid (sqKv1A). Biochemistry 40, 5942-5953.
53. Francke, O.F. (1979) Observations on the reproductive biology and life history of Megacormus gertschi Diaz (Scorpiones: Chactidae: Megacorminae). J. Arachnol. 7, 223-230.