Evidence map›Paper›PMID 26621745›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Role of protein dynamics in ion selectivity and allosteric coupling in the NaK channel.

Joshua B Brettmann, Darya Urusova, Marco Tonelli, Jonathan R Silva, Katherine A Henzler-Wildman

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.6field-weighted citation impact, top 30% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 21 citations in OpenAlex.

  1. High-Throughput MicroED for Probing Ion Channel Dynamics.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. TOK channels use the two gates in classical KFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  8. Review
  9. Conformational changes upon gating of KirBac1.1 into an open-activated state revealed by solid-state NMR and functional assays.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Joshua B BrettmannDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110;
Darya UrusovaDepartment of Biomedical Engineering, Washington University in Saint Louis, St. Louis, MO 63130;
Marco TonelliDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706.
Jonathan R SilvaDepartment of Biomedical Engineering, Washington University in Saint Louis, St. Louis, MO 63130;
Katherine A Henzler-WildmanDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110; Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706 henzlerwildm@wisc.edu.
Washington University in St. Louis · USUniversity of Wisconsin–Madison · US

Funding

WATER DISTRIB:PHYSICAL PROPERT:PIZZA &LMPS MOZZARELLA CHEESES:EARLY STAGE MATURP41RR002301 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 1985 to 2011
$13.0M
TR&D 3: TECHNOLOGY DEVELOPMENT FOR NMR STUDIES OF SMALL MOLECULES (METABOLOMICS, NATURAL PRODUCTS, METABOLITE-PROTEIN INTERACTIONS) pp.537-585 P41GM103399 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2012 to 2019
$9.4M
Integrated state-of-the-art LC-MS/NMR system for the University of WisconsinS10RR025062 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2008 to 2008
$1.7M
CONFORMATIONAL DYNAMICS IN ION CHANNEL SELECTIVITY AND GATINGR01GM116047 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI HENZLER-WILDMAN, KATHERINE ANNE · 2015 to 2018
$1.2M
Upgrade of the NMRFAM 750 MHz NMR SpectrometerS10RR029220 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2010 to 2010
$766k
NMR Spectrometer System Optimized for Direct 13C or 15N DetectionS10RR023438 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2008 to 2008
$500k
CONSOLE UPGRADES FOR NMR FACILITYS10RR008438 · NCRR · UNIVERSITY OF WISCONSIN MADISON · PI MARKLEY, JOHN L · 1993 to 1993
–
WIDE-BORE 9.4 TESLA NMR SPECTROMETER FOR UW-MADISONS10RR002781 · NCRR · UNIVERSITY OF WISCONSIN MADISON · PI MARKLEY, JOHN L · 1986 to 1986
–
NCRR NIH HHS P41 RR002301NCRR NIH HHS P41RR002301NCRR NIH HHS S10 RR002781NCRR NIH HHS S10 RR008438NCRR NIH HHS S10 RR023438NCRR NIH HHS S10RR023438NCRR NIH HHS S10 RR025062NCRR NIH HHS S10RR025062NCRR NIH HHS S10 RR029220NCRR NIH HHS S10RR029220NIGMS NIH HHS P41 GM103399NIGMS NIH HHS P41GM103399NIGMS NIH HHS R01 GM116047
6 · The paper itself

Abstract

Flux-dependent inactivation that arises from functional coupling between the inner gate and the selectivity filter is widespread in ion channels. The structural basis of this coupling has only been well characterized in KcsA. Here we present NMR data demonstrating structural and dynamic coupling between the selectivity filter and intracellular constriction point in the bacterial nonselective cation channel, NaK. This transmembrane allosteric communication must be structurally different from KcsA because the NaK selectivity filter does not collapse under low-cation conditions. Comparison of NMR spectra of the nonselective NaK and potassium-selective NaK2K indicates that the number of ion binding sites in the selectivity filter shifts the equilibrium distribution of structural states throughout the channel. This finding was unexpected given the nearly identical crystal structure of NaK and NaK2K outside the immediate vicinity of the selectivity filter. Our results highlight the tight structural and dynamic coupling between the selectivity filter and the channel scaffold, which has significant implications for channel function. NaK offers a distinct model to study the physiologically essential connection between ion conduction and channel gating.

Indexed as

Allosteric RegulationBacillus cereusCrystallography, X-RayIon Channel GatingIonsMagnetic Resonance SpectroscopyMutant ProteinsPoint MutationPotassiumPotassium ChannelsProtein FoldingProtein Structure, SecondarySolutionsTemperatureTime FactorsIonsMutant ProteinsPotassiumPotassium ChannelsSolutionsion channelsmembrane proteinprotein dynamicssolution NMR

Identifiers

PMID26621745
PMCPMC4687598
OpenAlexW2191604030

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.