Charybdotoxin

Charybdotoxin is a protein toxin that is produced by the Leiurus quinquestriatus scorpion. It is a potent inhibitor of calcium-activated potassium channels, which are important for the regulation of cellular excitability.

Structure

Charybdotoxin is a small protein composed of 37 amino acids. It has a compact, globular structure stabilized by three disulfide bonds. The surface of the protein is characterized by a large number of hydrophobic residues, which are thought to interact with the lipid bilayer of the cell membrane.

Function

Charybdotoxin blocks the calcium-activated potassium channels by binding to the outer mouth of the channel. This prevents the flow of potassium ions out of the cell, leading to an increase in cellular excitability. The toxin is highly selective for these channels, and does not affect other types of potassium channels.

Clinical significance

Due to its ability to block calcium-activated potassium channels, charybdotoxin has potential therapeutic applications. It could be used to treat conditions such as asthma, hypertension, and certain types of cancer, where these channels are known to play a role.

See also

• Scorpion venom
• Potassium channel
• Calcium-activated potassium channel
• Leiurus quinquestriatus

References

Charybdotoxin Resources
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