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

O Castañeda, V Sotolongo, A M Amor, R Stöcklin, A J Anderson, A L Harvey, A Engström, C Wernstedt, E Karlsson

Research output: Contribution to journalArticlepeer-review

228 Citations (Scopus)


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 languageEnglish
Pages (from-to)603-613
Number of pages11
Issue number5
Publication statusPublished - May 1995


  • amino acid sequence
  • amino acids
  • animals
  • cnidarian venoms
  • molecular sequence data
  • potassium channel blockers
  • potassium channels
  • rats
  • sea anemones
  • synaptosomes


Dive into the research topics of 'Characterization of a potassium channel toxin from the Caribbean Sea anemone Stichodactyla helianthus'. Together they form a unique fingerprint.

Cite this