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The study identifies specific physicochemical properties, including hydrophobicity at residue 656 and an aromatic group at residue 652, required for high-affinity drug binding and blockade of the hERG channel.
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Fernández et al. (2004) studied hERG channel block. Site-directed mutagenesis of Tyr-652 and Phe-656 vs. Wild-type hERG channels was evaluated on Channel block potency by cisapride, terfenadine, and MK-499.
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