Format

Send to

Choose Destination
Biochemistry (Mosc). 2015 Dec;80(13):1764-99. doi: 10.1134/S0006297915130118.

Diversity of Potassium Channel Ligands: Focus on Scorpion Toxins.

Author information

1
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, 117997, Russia. aleksey.kuzmenkov@gmail.com.

Abstract

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).

PMID:
26878580
DOI:
10.1134/S0006297915130118
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Biochemistry (Moscow)
Loading ...
Support Center