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Role of Disulfide Bonds in the Structure and Potassium Channel Blocking Activity of ShK Toxin †

✍ Scribed by Pennington, Michael W.; Lanigan, Mark D.; Kalman, Katalin; Mahnir, Vladimir M.; Rauer, Heiko; McVaugh, Cheryl T.; Behm, David; Donaldson, Denise; Chandy, K. George; Kem, William R.; Norton, Raymond S.

Book ID
126429992
Publisher
American Chemical Society
Year
1999
Tongue
English
Weight
205 KB
Volume
38
Category
Article
ISSN
0006-2960

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Assignment of the three disulfide bonds
Assignment of the three disulfide bonds in ShK toxin: A potent potassium channel inhibitor from the sea anemoneStichodactyla helianthus
✍ Jan Pohl; Frantisek Hubalek; Michael E. Byrnes; Kurt R. Nielsen; Amina Woods; Mi 📂 Article 📅 1995 🏛 Springer Netherlands 🌐 English ⚖ 422 KB

ShK toxin, a 35-residue peptide isolated from the Caribbean sea anemone Stichodactyla helianthus, is a potent inhibitor of the Kv1.3 potassium channel in lymphocytes. The natural toxin contains three disulfide bonds. The disulfide pairings of the synthetic ShK toxin were elucidated as a prerequisite