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Solution structure of ShK toxin, a novel potassium channel inhibitor from a sea anemone

✍ Scribed by Tudor, Jane E. ;Pallaghy, Paul K. ;Pennington, Michael W. ;Norton, Raymond S.

Book ID
109964729
Publisher
Nature Publishing Group
Year
1996
Tongue
English
Weight
514 KB
Volume
3
Category
Article
ISSN
1545-9993

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Sea anemones possess small K-channel-blocking peptides about the same size as the scorpion K-channel toxins. We have estimated the secondary structure content (33% helix, 26% ]3-sheet) of one of these toxins, ShK toxin, using CD, Raman, and FTIR spectroscopy. A hypothetical 3D structure of the pepti

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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