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A novel inhibitor of voltage-gated K + channels has been purified to homogeneity from the venom of the black scorpion Orthochirus scrobiculosus. This toxin, named OsK2, has been characterized as a 28-residue peptide, containing six conserved cysteine residues and was shown to be a potent and selective blocker of Kv1.2 channels (K d = 97 nM). OsK2 is the second member of the 13th subfamily...
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