Structure and function of the potassium channel inhibitor from black scorpion venom

E. V. Grishin, Yu V. Korolkova, S. A. Kozlov, A. V. Lipkin, E. D. Nosyreva, K. A. Pluzhnikov, S. V. Sukhanov, T. M. Volkova

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

A novel inhibitor of K+ channels has been purified from the venom of the Central Asian scorpion Orlhochirus scrobiculosus. For this polypeptide toxin (OsK-1) with molecular mass 4205.7 Da complete amino acid sequence was determined by Edman degradation and C-terminal amino acid analysis, and was confirmed by cloning and sequencing of the toxin cDNA. OsK-1 consists of 38 amino acid residues and possesses high sequence homology with agiotoxin, kaliotoxin and some homology with other known K+-channel blockers from different scorpion venoms. The toxin was shown to block small-conductance Ca++-activated K+-channels in neuroblastomaxglioma NG 108-15 hybrid cells (Kd=1.4 × 10-7 M) which are insensitive to apamin and sensitive to charybdotoxin. The effect of OsK-1 was reversible and concentration dependent.

Original languageEnglish (US)
Pages (from-to)2105-2109
Number of pages5
JournalPure and Applied Chemistry
Volume68
Issue number11
DOIs
StatePublished - Nov 1996

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

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    Grishin, E. V., Korolkova, Y. V., Kozlov, S. A., Lipkin, A. V., Nosyreva, E. D., Pluzhnikov, K. A., Sukhanov, S. V., & Volkova, T. M. (1996). Structure and function of the potassium channel inhibitor from black scorpion venom. Pure and Applied Chemistry, 68(11), 2105-2109. https://doi.org/10.1351/pac199668112105