Evidence map›Paper›PMID 26100907›Full record

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

A structural, functional, and computational analysis suggests pore flexibility as the base for the poor selectivity of CNG channels.

Luisa Maria Rosaria Napolitano, Ina Bisha, Matteo De March, Arin Marchesi, Manuel Arcangeletti, Nicola Demitri, Monica Mazzolini, Alex Rodriguez, Alessandra Magistrato, Silvia Onesti and 2 more

Abstract 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 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Collective Domain Motion Facilitates Water Transport in SGLT1.International journal of molecular sciences · 2023
    Article
  5. Mechanism of Calcium Permeation in a Glutamate Receptor Ion Channel.Journal of chemical information and modeling · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. CNG channel structure, function, and gating: a tale of conformational flexibility.Pflugers Archiv : European journal of physiology · 2021
    Review
  11. Article
  12. Nonselective cation permeation in an AMPA-type glutamate receptor.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

12 authors.

Luisa Maria Rosaria NapolitanoStructural Biology Laboratory, Elettra-Sincrotrone Trieste S.C.p.A., Basovizza, Trieste 34149, Italy;
Ina BishaInternational School for Advanced Studies, Trieste 34136, Italy;
Matteo De MarchStructural Biology Laboratory, Elettra-Sincrotrone Trieste S.C.p.A., Basovizza, Trieste 34149, Italy;
Arin MarchesiInternational School for Advanced Studies, Trieste 34136, Italy;
Manuel ArcangelettiInternational School for Advanced Studies, Trieste 34136, Italy;
Nicola DemitriStructural Biology Laboratory, Elettra-Sincrotrone Trieste S.C.p.A., Basovizza, Trieste 34149, Italy;
Monica MazzoliniInternational School for Advanced Studies, Trieste 34136, Italy;
Alex RodriguezInternational School for Advanced Studies, Trieste 34136, Italy;
Alessandra MagistratoInternational School for Advanced Studies, Trieste 34136, Italy; National Research Council-Institute of Materials (CNR-IOM)-Democritos National Simulation Center c/o International School for Advanced Studies, Trieste 34136, Italy.
Silvia OnestiStructural Biology Laboratory, Elettra-Sincrotrone Trieste S.C.p.A., Basovizza, Trieste 34149, Italy; torre@sissa.it laio@sissa.it silvia.onesti@elettra.eu.
Alessandro LaioInternational School for Advanced Studies, Trieste 34136, Italy; torre@sissa.it laio@sissa.it silvia.onesti@elettra.eu.
Vincent TorreInternational School for Advanced Studies, Trieste 34136, Italy; torre@sissa.it laio@sissa.it silvia.onesti@elettra.eu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclic nucleotide-gated (CNG) ion channels, despite a significant homology with the highly selective K(+) channels, do not discriminate among monovalent alkali cations and are permeable also to several organic cations. We combined electrophysiology, molecular dynamics (MD) simulations, and X-ray crystallography to demonstrate that the pore of CNG channels is highly flexible. When a CNG mimic is crystallized in the presence of a variety of monovalent cations, including Na(+), Cs(+), and dimethylammonium (DMA(+)), the side chain of Glu66 in the selectivity filter shows multiple conformations and the diameter of the pore changes significantly. MD simulations indicate that Glu66 and the prolines in the outer vestibule undergo large fluctuations, which are modulated by the ionic species and the voltage. This flexibility underlies the coupling between gating and permeation and the poor ionic selectivity of CNG channels.

Indexed as

Protein ConformationAmino Acid SequenceAnimalsBacterial ProteinsCations, MonovalentCattleCesiumCrystallography, X-RayCyclic Nucleotide-Gated Cation ChannelsFemaleIon Channel GatingIon TransportMembrane PotentialsMolecular Dynamics SimulationMolecular Sequence DataMutant ProteinsBacterial ProteinsCations, MonovalentCesiumCNGA1 protein, bovineCyclic Nucleotide-Gated Cation ChannelsMutant ProteinsSodiumCNG channelsMD simulationspore flexibilityX-ray crystallography

Identifiers

PMID26100907
PMCPMC4500290

What OpenQuestion holds

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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.