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- W2026811787 abstract "The four voltage sensors in Cav channels have distinct amino acid sequences, raising fundamental questions about their relative contributions to the function and regulation of the channel. Studies of Kv channels identified a S3b-S4 helix-turn-helix motif, termed paddle motif, which moves at the protein-lipid interface interface to drive activation of the voltage-sensors. This motif is an important pharmacological target for amphipathic neurotoxins and it has been suggested that is conserved in Cav and other voltage-gated ion channels. Here we show that the four S3b-S4 paddle motifs within the Cav channel could be transplanted into four-fold symmetric Kv channel to individually examine their contributions to the kinetics of voltage sensor activation and regulation by toxins." @default.
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- W2026811787 date "2009-02-01" @default.
- W2026811787 modified "2023-09-26" @default.
- W2026811787 title "Voltage-sensor Pharmacology Of Voltage-activated Calcium Channels (cav)" @default.
- W2026811787 doi "https://doi.org/10.1016/j.bpj.2008.12.862" @default.
- W2026811787 hasPublicationYear "2009" @default.
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