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 of short-chain K(+) channel-blocking peptides known thus far and is therefore called alpha-KTx 13.2.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1006/bbrc.2001.5492 | DOI Listing |
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!