Contributions of a negatively charged residue in the hydrophobic domain of the IRK1 inwardly rectifying K+ channel to K(+)-selective permeation.
Inwardly rectifying K+ channels are highly selective for K+ ions and show strong interaction with ions in the pore. Both features are important for the physiological functions of these channels and pose intriguing mechanistic questions of ion permeation. The aspartate residue in the second putative transmembrane segment of the IRK1 inwardly rectifying K+ channel, previously implicated in inward rectification gating due to cytoplasmic Mg2+ and polyamine block, is found in this study to be crucial for the channel's ability to distinguish between K+ and Rb+ ions. Mutation of this residue also perturbs the interaction between the channel pore and the Sr2+ blocking ion. Our studies suggest that this aspartate residue contributes to a selectivity filter near the cytoplasmic end of the pore.
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Department of Physiology, University of California, San Francisco 94143-0724, USA.
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D000818:Animals; D001665:Binding Sites; D055592:Biophysical Phenomena; D001703:Biophysics; D003001:Cloning, Molecular; D003593:Cytoplasm / Q000378:metabolism; D004563:Electrochemistry; D005260:Female; D066298:In Vitro Techniques; D017136:Ion Transport; D007700:Kinetics; D015394:Molecular Structure; D016297:Mutagenesis, Site-Directed; D009865:Oocytes; D010539:Permeability; D017354:Point Mutation; D011188:Potassium / Q000378:metabolism*; D015221:Potassium Channels / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D024661:Potassium Channels, Inwardly Rectifying; D012413:Rubidium / Q000378:metabolism; D013324:Strontium / Q000378:metabolism; D014982:Xenopus laevis
D015221:Potassium Channels; D024661:Potassium Channels, Inwardly Rectifying; D012413:Rubidium; D011188:Potassium; D013324:Strontium