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.
Original language | English |
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Pages (from-to) | 603-613 |
Number of pages | 11 |
Journal | Toxicon |
Volume | 33 |
Issue number | 5 |
DOIs | |
Publication status | Published - May 1995 |
Keywords
- amino acid sequence
- amino acids
- animals
- cnidarian venoms
- molecular sequence data
- potassium channel blockers
- potassium channels
- rats
- sea anemones
- synaptosomes