Abstract

The overall sequence similarity between the voltage-activated K + channels and cyclic nucleotide-gated ion channels from retinal and olfactory neurons suggests that they arose from a common ancestor. On the basis of sequence comparisons, mutations were introduced into the pore of a voltage-activated K + channel. These mutations confer the essential features of ion conduction in the cyclic nucleotide-gated ion channels; the mutant K + channels display little selectivity among monovalent cations and are blocked by divalent cations. The property of K + selectivity is related to the presence of two amino acids that are absent from the pore-forming region of the cyclic nucleotide-gated channels. These data demonstrate that very small differences in the primary structure of an ion channel can account for extreme functional diversity, and they suggest a possible connection between the pore-forming regions of K + , Ca 2+ , and cyclic nucleotide-gated ion channels.

Keywords

Ion channelCyclic nucleotide-gated ion channelDivalentNucleotideBiophysicsChemistryIonMutantSelectivityIon transporterCyclic nucleotideCrystallographyBiologyBiochemistryGene

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Year
1992
Type
article
Volume
258
Issue
5085
Pages
1152-1155
Citations
484
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Lise Heginbotham, Tatiana Abramson, Roderick MacKinnon (1992). A Functional Connection Between the Pores of Distantly Related Ion Channels as Revealed by Mutant K <sup>+</sup> Channels. Science , 258 (5085) , 1152-1155. https://doi.org/10.1126/science.1279807

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DOI
10.1126/science.1279807