ArticleNature structural & molecular biology2009
Structural analysis of ion selectivity in the NaK channel.
Article in Nature structural & molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
55 citing papers in PubMed.
- Atomistic mechanism of non-selective cation permeation in cyclic nucleotide-gated CNGA1 ion channel by molecular dynamics simulations.Communications biology · 2025Article
- High-Throughput MicroED for Probing Ion Channel Dynamics.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Full opening of helix bundle crossing does not lead to NaK channel activation.The Journal of general physiology · 2022Article
- Molecular Events behind the Selectivity and Inactivation Properties of Model NaK-Derived Ion Channels.International journal of molecular sciences · 2022Article
- Studying membrane proteins with MicroED.Biochemical Society transactions · 2022Article
- Ion-dependent structure, dynamics, and allosteric coupling in a non-selective cation channel.Nature communications · 2021Article
- Article
- Nonselective cation permeation in an AMPA-type glutamate receptor.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Inferring functional units in ion channel pores via relative entropy.European biophysics journal : EBJ · 2021Article
- Studying Membrane Protein Structures by MicroED.Methods in molecular biology (Clifton, N.J.) · 2021Article
- High-Resolution Structures of KHandbook of experimental pharmacology · 2021Article
- Beyond protein structure determination with MicroED.Current opinion in structural biology · 2020Review
- The structure of a potassium-selective ion channel reveals a hydrophobic gate regulating ion permeation.IUCrJ · 2020Article
- Article
- Ion permeation in potassium ion channels.Acta crystallographica. Section D, Structural biology · 2020Review
- Selectivity filter modalities and rapid inactivation of the hERG1 channel.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Solving a new R2lox protein structure by microcrystal electron diffraction.Science advances · 2019Article
- Equilibria between the KProtein & cell · 2019Article
- Predicting Site-Binding Modes of Ions and Water to Nucleic Acids Using Molecular Solvation Theory.Journal of the American Chemical Society · 2019Article
- Mapping the Conformational Landscape of Glutamate Receptors Using Single Molecule FRET.Trends in neurosciences · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Here we present a detailed characterization of ion binding in the NaK pore using the high-resolution structures of NaK in complex with various cations. These structures reveal four ion binding sites with similar chemical environments but vastly different ion preference. The most nonselective of all is site 3, which is formed exclusively by backbone carbonyl oxygen atoms and resides deep within the selectivity filter. Additionally, four water molecules in combination with four backbone carbonyl oxygen atoms are seen to participate in K(+) and Rb(+) ion chelation, at both the external entrance and the vestibule of the NaK filter, confirming the channel's preference for an octahedral ligand configuration for K(+) and Rb(+) binding. In contrast, Na(+) binding in the NaK filter, particularly at site 4, utilizes a pyramidal ligand configuration that requires the participation of a water molecule in the cavity. Therefore, the ability of the NaK filter to bind both Na(+) and K(+) ions seemingly arises from the ions' ability to use the existing environment in unique ways, rather than from any structural rearrangements of the filter itself.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.