Diversity of potassium channel ligands: focus on scorpion toxinsстатья

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Дата последнего поиска статьи во внешних источниках: 20 июня 2016 г.

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[1] Kuzmenkov A. I., Grishin E. V., Vassilevski A. A. Diversity of potassium channel ligands: focus on scorpion toxins // Biochemistry (Moscow). — 2015. — Vol. 80, no. 13. — P. 1764–1799. Potassium (K+) channels are a widespread superfamily of integral membrane proteins that mediate selective transport of K+ ions through the cell membrane. They have been found in all living organisms from bacteria to higher multicellular animals, including humans. Not surprisingly, K+ channels bind ligands of different nature, such as metal ions, low molecular mass compounds, venom-derived peptides, and antibodies. Functionally these substances can be K+ channel pore blockers or modulators. Representatives of the first group occlude the channel pore, like a cork in a bottle, while the second group of ligands alters the operation of channels without physically blocking the ion current. A rich source of K+ channel ligands is venom of different animals: snakes, sea anemones, cone snails, bees, spiders, and scorpions. More than a half of the known K+ channel ligands of polypeptide nature are scorpion toxins (KTx), all of which are pore blockers. These compounds have become an indispensable molecular tool for the study of K+ channel structure and function. A recent special interest is the possibility of toxin application as drugs to treat diseases involving K+ channels or related to their dysfunction (channelopathies). [ DOI ]

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