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• W2083809358 abstract "The cardiac hERG K+ channel constitutes a long-standing and expensive antitarget for the drug industry. From a study of the flexibility of hERG around its internal binding cavity, we have developed a new structural model of drug binding to hERG, which involves binding orthogonal to the pore channel and therefore can exploit the up to 4-fold symmetry of the tetrameric channel. This binding site has a base formed by four tyrosine side chains that complement reported ligand-based pharmacophores. The model is able to rationalize reduced hERG potency in matched molecular pair studies and suggests design guidelines to optimize against hERG not relying simply on lipophilicity reduction. The binding model also suggests a molecular mechanism for the link between high-affinity hERG binding and C-type inactivation." @default.
• W2083809358 created "2016-06-24" @default.
• W2083809358 creator A5002086598 @default.
• W2083809358 creator A5058544519 @default.
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• W2083809358 date "2009-06-17" @default.
• W2083809358 modified "2023-09-23" @default.
• W2083809358 title "Side Chain Flexibilities in the Human Ether-a-go-go Related Gene Potassium Channel (hERG) Together with Matched-Pair Binding Studies Suggest a New Binding Mode for Channel Blockers" @default.
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• W2083809358 doi "https://doi.org/10.1021/jm900002x" @default.
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• W2083809358 hasPublicationYear "2009" @default.
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