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- W2006129103 abstract "Divalent cation blockade of cGMP-gated channels in photoreceptor cells ensures the low open channel noise required for a highly sensitive visual transduction process. This study identifies a divalent cation-binding site in the pore of a retinal cGMP-gated channel expressed in Xenopus oocytes. Substitution of a specific glutamate residue by a neutral amino acid renders the channel insensitive to external Mg2+ and Ca2+ and affects the conduction of Na+. The mutated channels remain sensitive to internal divalent cations. These results place the glutamate residue in the ion conduction pathway close to the extracellular surface." @default.
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- W2006129103 title "Identification of an external divalent cation-binding site in the pore of a cGMP-activated channel" @default.
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- W2006129103 doi "https://doi.org/10.1016/0896-6273(93)90150-p" @default.
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