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• W2023897242 startingPage "411" @default.
• W2023897242 abstract "Voltage-gated K+ channels contain a central pore domain and four surrounding voltage-sensing domains. How and where changes in the structure of the voltage-sensing domains couple to the pore domain so as to gate ion conduction is not understood. The crystal structure of KcsA, a bacterial K+ channel homologous to the pore domain of voltage-gated K+ channels, provides a starting point for addressing this question. Guided by this structure, we used tryptophan-scanning mutagenesis on the transmembrane shell of the pore domain in the Shaker voltage-gated K+ channel to localize potential protein-protein and protein-lipid interfaces. Some mutants cause only minor changes in gating and when mapped onto the KcsA structure cluster away from the interface between pore domain subunits. In contrast, mutants producing large changes in gating tend to cluster near this interface. These results imply that voltage-sensing domains interact with localized regions near the interface between adjacent pore domain subunits." @default.
• W2023897242 created "2016-06-24" @default.
• W2023897242 creator A5003818735 @default.
• W2023897242 creator A5020708402 @default.
• W2023897242 creator A5060415836 @default.
• W2023897242 date "2000-02-01" @default.
• W2023897242 modified "2023-10-17" @default.
• W2023897242 title "A Localized Interaction Surface for Voltage-Sensing Domains on the Pore Domain of a K+ Channel" @default.
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• W2023897242 doi "https://doi.org/10.1016/s0896-6273(00)80904-6" @default.
• W2023897242 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10719895" @default.
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