Evidence map›Paper›PMID 27439597›Full record

ArticleScientific reports2016

The Molecular Mechanism of Opening the Helix Bundle Crossing (HBC) Gate of a Kir Channel.

Xuan-Yu Meng, Shengtang Liu, Meng Cui, Ruhong Zhou, Diomedes E Logothetis

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

24 citing papers in PubMed, 31 citations in OpenAlex.

  1. Similarity of the ion occupations of KChannels (Austin, Tex.) · 2026
    Article
  2. PIPbioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Allosteric coupling between PIPProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Understanding Ion Channel Gating Mechanisms by Molecular Dynamics Simulations.Advances in experimental medicine and biology · 2026
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Palmitoylation of the KProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. Article
  19. Article
  20. Conduction through a narrow inward-rectifier KThe Journal of general physiology · 2019
    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 3 institutions in 2 countries.

Xuan-Yu MengInstitute of Quantitative Biology and Medicine, SRMP and RAD-X, Collaborative Innovation Center of Radiation Medicine of Jiangsu Higher Education Institutions, Soochow University, Suzhou 215123, China.
Shengtang LiuInstitute of Quantitative Biology and Medicine, SRMP and RAD-X, Collaborative Innovation Center of Radiation Medicine of Jiangsu Higher Education Institutions, Soochow University, Suzhou 215123, China.
Meng CuiDepartment of Physiology and Biophysics, Virginia Commonwealth University, School of Medicine, Richmond, Virginia.
Ruhong ZhouInstitute of Quantitative Biology and Medicine, SRMP and RAD-X, Collaborative Innovation Center of Radiation Medicine of Jiangsu Higher Education Institutions, Soochow University, Suzhou 215123, China.
Diomedes E LogothetisDepartment of Physiology and Biophysics, Virginia Commonwealth University, School of Medicine, Richmond, Virginia.
Virginia Commonwealth University · USIBM Research - Thomas J. Watson Research Center · USSoochow University · CN

Funding

Structural Determinants of PIP2 RegulationR01HL059949 · NHLBI · VIRGINIA COMMONWEALTH UNIVERSITY · PI Leigh Daniel Plant · 1998 to 2026
$11.6M
Modulation of Kir Channel Function by PhosphorylationR01HL090882 · NHLBI · VIRGINIA COMMONWEALTH UNIVERSITY · PI LOGOTHETIS, DIOMEDES E. · 2009 to 2012
$1.5M
NHLBI NIH HHS R01 HL059949NHLBI NIH HHS R01 HL090882
6 · The paper itself

Abstract

Inwardly rectifying K(+) (Kir) channels, serving as natural molecular nanomachines, transport potassium ions across the plasma membrane of the cell. Along the ion permeation pathway, three relatively narrow regions (the selectivity filter (SF), the inner helix bundle crossing (HBC), and the cytosolic G loop) may serve as gates to control ion permeation. Our previous molecular dynamics simulations based on the crystal structure of a Kir3.1 chimera revealed the possible gating mechanism of the G loop gate. Here, we introduced a proline mutation in the inner helix and obtained a channel model of the open HBC gate. The open HBC gate reaches 0.6 nm in diameter, which allows partial hydrated K(+) ions to pass through. During the gating process, both the transmembrane helices TM1 and TM2 cooperatively rotate in a counterclockwise direction (viewed from the extracellular side) with the aid of the phospholipid PIP2. Only when all the transmembrane helices adopt a counterclockwise rotation, the HBC gate can be stabilized in the open state. We estimate that introduction of the proline mutation decreases the energy required to open the HBC gate by about 1.4 kcal/mol (ΔΔG).

Indexed as

Cell MembraneCrystallography, X-RayEscherichia coliG Protein-Coupled Inwardly-Rectifying Potassium ChannelsHumansHydrophobic and Hydrophilic InteractionsIonsMagnetospirillumMolecular Dynamics SimulationMotionMutationPhospholipidsPotassiumPrincipal Component AnalysisProtein BindingProtein DomainsG Protein-Coupled Inwardly-Rectifying Potassium ChannelsIonsPhospholipidsPotassium

Identifiers

PMID27439597
PMCPMC4954981
OpenAlexW2487437738

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.