Abstract.
The venoms of predatory cone snails harbor a rich repertoire of peptide toxins that are valuable research tools, but recently have also proven to be useful drugs. Among the conotoxins with several disulfide bridges, the O-superfamily toxins are characterized by a conserved cysteine knot pattern: C-C-CC-C-C. While ω-conotoxins and κ-conotoxins block Ca2+ and K+ channels, respectively, the closely related δ- and μO-conotoxins affect voltage-gated Na+ channels (Nav channels). δ-conotoxins mainly remove the fast inactivation of Nav channels and, thus, functionally resemble long-chain scorpion α-toxins. μO-conotoxins are functionally similar to μ-conotoxins, since they inhibit the ion flow through Nav channels. Recent results from functional and structural assays have gained insight into the underlying molecular mechanisms. Both types of toxins are voltage-sensor toxins interfering with the voltage-sensor elements of Nav channels.
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Received 27 December 2006; received after revision 30 January 2007; accepted 19 February 2007
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Heinemann, S.H., Leipold, E. Conotoxins of the O-superfamily affecting voltage-gated sodium channels. Cell. Mol. Life Sci. 64, 1329–1340 (2007). https://doi.org/10.1007/s00018-007-6565-5
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DOI: https://doi.org/10.1007/s00018-007-6565-5