ArticleBiophysical journal2012
Nonselective conduction in a mutated NaK channel with three cation-binding sites.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 16 citations in OpenAlex.
- Early Steps in C-Type Inactivation of the hERG Potassium Channel.Journal of chemical information and modeling · 2023Article
- Selectivity filter modalities and rapid inactivation of the hERG1 channel.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Direct knock-on of desolvated ions governs strict ion selectivity in KNature chemistry · 2018Article
- Energetics of Ion Permeation in an Open-Activated TRPV1 Channel.Biophysical journal · 2016Article
- A structural, functional, and computational analysis suggests pore flexibility as the base for the poor selectivity of CNG channels.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- K(+) and Na(+) conduction in selective and nonselective ion channels via molecular dynamics simulations.Biophysical journal · 2013Review
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The NaK channel is a cation-selective protein with similar permeability for K(+) and Na(+) ions. Crystallographic structures are available for the wild-type and mutated NaK channels with different numbers of cation-binding sites. We have performed a comparison between the potentials of mean force governing the translocation of K(+) ions and mixtures of one Na(+) and three K(+) ions in a mutated NaK channel with only three cation-binding sites (NaK-CNG). Since NaK-CNG is not selective for K(+) over Na(+), analysis of its multi-ion potential energy surfaces can provide clues about how selectivity originates. Comparison of the potentials of mean force of NaK-CNG and K(+)-selective channels yields observations that strongly suggest that the number of contiguous ion binding sites in a single-file mechanism is the key determinant of the channel's selectivity properties, as already proposed by experimental studies. We conclude that the presence of four binding sites in K(+)-selective channels is essential for highly selective and efficient permeation of K(+) ions, and that a key difference between K(+)-selective and nonselective channels is the absence/presence of a binding site for Na(+) ions at the boundary between S2 and S3 in the context of multi-ion permeation events.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.