Conotoxins of the O-superfamily affecting voltage-gated sodium channels.
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 omega-conotoxins and kappa-conotoxins block Ca(2+) and K(+) channels, respectively, the closely related delta- and microO-conotoxins affect voltage-gated Na(+) channels (Na(v) channels). delta-conotoxins mainly remove the fast inactivation of Na(v) channels and, thus, functionally resemble long-chain scorpion alpha-toxins. microO-conotoxins are functionally similar to micro-conotoxins, since they inhibit the ion flow through Na(v) 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 Na(v) channels.
Heinemann
S H
SH
Center of Molecular Biomedicine, Department of Biophysics, Friedrich Schiller University Jena, Drackendorfer Str 1, Jena, Germany. Stefan.H.Heinemann@uni-jena.de
Leipold
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D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D020916:Conotoxins / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D018482:Muscle, Skeletal / Q000378:metabolism; D009474:Neurons / Q000378:metabolism; D010802:Phylogeny; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D015222:Sodium Channels / Q000378:metabolism*
D020916:Conotoxins; D021122:Protein Subunits; D015222:Sodium Channels