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Solution structure of Pi4, a short four-disulfide-bridged scorpion toxin specific of potassium channels

✍ Scribed by J. Iñaki Guijarro; Sarrah M'Barek; Froylan Gómez-Lagunas; Damien Garnier; Hervé Rochat; Jean-Marc Sabatier; Lourrival D. Possani; Muriel Delepierre

Book ID
119824220
Publisher
Cold Spring Harbor Laboratory Press
Year
2003
Tongue
English
Weight
288 KB
Volume
12
Category
Article
ISSN
0961-8368

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Solution structure of P01, a natural sco
Solution structure of P01, a natural scorpion peptide structurally analogous to scorpion toxins specific for apamin-sensitive potassium channel
✍ Blanc, E.; Fremont, V.; Sizun, P.; Meunier, S.; Van Rietschoten, J.; Thevand, A. 📂 Article 📅 1996 🏛 John Wiley and Sons 🌐 English ⚖ 832 KB

The venom of the North African scorpion Androctonus mauretanicus mauretanicus possesses numerous highly active neurotoxins that specifically bind to various ion channels. One of these, P05, has been found to bind specifically to calcium-activated potassium channels and also to compete with apamin, a

Solution structure of maurotoxin, a scor
Solution structure of maurotoxin, a scorpion toxin from Scorpio maurus, with high affinity for voltage-gated potassium channels
✍ E. Blanc; J.M. Sabatier; R. Kharrat; S. Meunier; M. El Ayeb; J. Van Rietschoten; 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 488 KB 👁 2 views

Maurotoxin (MTX), purified from the scorpionid Scorpio maurus is a potent ligand for potassium channels. It shows a broad specificity as being active on Kv1.1 (Kd ‫؍‬ 37 nM), Kv1.2 (Kd ‫؍‬ 0.8 nM), Kv1.3 (Kd ‫؍‬ 150 nM) voltage-gated potassium channels, as well as on small-conductance calcium-activa