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WIN 17317-3, a New High-Affinity Probe for Voltage-Gated Sodium Channels †

✍ Scribed by Wanner, Siegmund G.; Glossmann, Hartmut; Knaus, Hans-Günther; Baker, Robert; Parsons, William; Rupprecht, Kathleen M.; Brochu, Richard; Cohen, Charles J.; Schmalhofer, William; Smith, McHardy; Warren, Vivien; Garcia, Maria L.; Kaczorowski, Gregory J.

Book ID
127211153
Publisher
American Chemical Society
Year
1999
Tongue
English
Weight
120 KB
Volume
38
Category
Article
ISSN
0006-2960

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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