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  • Title: Glycine 30 in iberiotoxin is a critical determinant of its specificity for maxi-K versus K(V) channels.
    Author: Schroeder N, Mullmann TJ, Schmalhofer WA, Gao YD, Garcia ML, Giangiacomo KM.
    Journal: FEBS Lett; 2002 Sep 11; 527(1-3):298-302. PubMed ID: 12220678.
    Abstract:
    Iberiotoxin (IbTX) is a remarkably selective alpha-K toxin peptide (alpha-KTx) inhibitor of the maxi-K channel. In contrast, the highly homologous charybdotoxin inhibits both the maxi-K and K(V)1.3 channels with similar high affinity. The present study investigates the molecular basis for this specificity through mutagenesis of IbTX. The interactions of mutated peptides with maxi-K and K(V)1.3 channels were monitored through dose-dependent displacement of specifically bound iodinated alpha-KTx peptides from membranes expressing these channels. Results of these studies suggest that the presence of a glycine at position 30 in IbTX is a major determinant of its specificity while the presence of four unique acidic residues in IbTX is not.
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