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

doi:10.1351/pac199668112105

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

Neuroscience

Research output: Contribution to journal › Article › peer-review

15 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 (K_d=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 language	English (US)
Pages (from-to)	2105-2109
Number of pages	5
Journal	Pure and Applied Chemistry
Volume	68
Issue number	11
DOIs	https://doi.org/10.1351/pac199668112105
State	Published - Nov 1996

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General Chemistry
General Chemical Engineering

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title = "Structure and function of the potassium channel inhibitor from black scorpion venom",

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.",

author = "Grishin, {E. V.} and Korolkova, {Yu V.} and Kozlov, {S. A.} and Lipkin, {A. V.} and Nosyreva, {E. D.} and Pluzhnikov, {K. A.} and Sukhanov, {S. V.} and Volkova, {T. M.}",

note = "Funding Information: This work was supported by the Russian foundation of Fundamental Research and International Science Foundation. We wish to acknowledge the help of Dr. Chertova E.N. for amino acid sequence determinations.",

year = "1996",

month = nov,

doi = "10.1351/pac199668112105",

language = "English (US)",

volume = "68",

pages = "2105--2109",

journal = "Pure and Applied Chemistry",

issn = "0033-4545",

publisher = "IUPAC Secretariat",

number = "11",

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T1 - Structure and function of the potassium channel inhibitor from black scorpion venom

AU - Grishin, E. V.

AU - Korolkova, Yu V.

AU - Kozlov, S. A.

AU - Lipkin, A. V.

AU - Nosyreva, E. D.

AU - Pluzhnikov, K. A.

AU - Sukhanov, S. V.

AU - Volkova, T. M.

N1 - Funding Information: This work was supported by the Russian foundation of Fundamental Research and International Science Foundation. We wish to acknowledge the help of Dr. Chertova E.N. for amino acid sequence determinations.

PY - 1996/11

Y1 - 1996/11

N2 - 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.

AB - 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.

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JO - Pure and Applied Chemistry

JF - Pure and Applied Chemistry

IS - 11

ER -

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

Abstract

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