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• W2023331462 abstract "At least five different types of voltage-gated Ca2+ channels exist in electrically excitable mammalian cells. Only one type, the family of L-type Ca2+ channels (L channels), contains high-affinity binding domains within their alpha 1-subunits for different chemical classes of drugs (Ca2+ channel antagonists; exemplified by isradipine, verapamil and diltiazem). Their stereoselective, high-affinity binding induces block of channel-mediated Ca2+ inward currents in heart and smooth muscle, resulting in antihypertensive, cardiodepressive and antiarrhythmic effects. Amino acids involved in drug binding have recently been identified using photoaffinity labelling, chimeric alpha 1-subunits and site-directed mutagenesis. Insertion of the drug-binding amino acids enabled the transfer of drug-sensitivity into Ca2+ channels that are insensitive to Ca2+ channel antagonists ('gain-of-function' approach). In this review, Jörg Striessing and colleagues summarize the present knowledge about the molecular architecture of L channel drug-binding domains and the implications for Ca2+ channel pharmacology and drug development." @default.
• W2023331462 created "2016-06-24" @default.
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• W2023331462 date "1998-03-01" @default.
• W2023331462 modified "2023-10-14" @default.
• W2023331462 title "Structural basis of drug binding to L Ca2+ channels" @default.
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• W2023331462 doi "https://doi.org/10.1016/s0165-6147(98)01171-7" @default.
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