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Characterization of a potassium channel toxin from the Caribbean Sea anemone Stichodactyla helianthus

Castañeda, O and Sotolongo, V and Amor, A M and Stöcklin, R and Anderson, A J and Harvey, A L and Engström, A and Wernstedt, C and Karlsson, E (1995) Characterization of a potassium channel toxin from the Caribbean Sea anemone Stichodactyla helianthus. Toxicon, 33 (5). pp. 603-613. ISSN 1879-3150

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Abstract

A peptide toxin, ShK, that blocks voltage-dependent potassium channels was isolated from the whole body extract of the Caribbean sea anemone Stichodactyla helianthus. It competes with dendrotoxin I and alpha-dendrotoxin for binding to synaptosomal membranes of rat brain, facilities acetylcholine release at an avian neuromuscular junction and suppresses K+ currents in rat dorsal root ganglion neurones in culture. Its amino acid sequence is R1SCIDTIPKS10RCTAFQCKHS20MKYRLSFCRK30TCGTC35. There is no homology with other K+ channel-blocking peptides, except for BgK from the sea anemone Bunodosoma granulifera. ShK and BgK appear to be in a different structural class from other toxins affecting K+ channels.