Evidence map›Paper›PMID 26743208›Full record

ArticleProgress in biophysics and molecular biology2016

Conformational changes of an ion-channel during gating and emerging electrophysiologic properties: Application of a computational approach to cardiac Kv7.1.

Ali Nekouzadeh, Yoram Rudy

Open access · hybridAbstract read
In one paragraph

Article in Progress in biophysics and molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.3field-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

5 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Article
  3. Hydrophobic gasket mutation produces gating pore currents in closed human voltage-gated proton channels.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  4. Article
  5. 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

2 authors at 1 institution in 1 country.

Ali NekouzadehCardiac Bioelectricity and Arrhythmia Center and Departments of Biomedical Engineering and Cell Biology & Physiology, Washington University in St. Louis, 290 Whitaker Hall, 1 Brooking Dr., St. Louis, MO 63130, USA. Electronic address: nekouzadeh@wustl.edu.
Yoram RudyCardiac Bioelectricity and Arrhythmia Center and Departments of Biomedical Engineering and Cell Biology & Physiology, Washington University in St. Louis, 290 Whitaker Hall, 1 Brooking Dr., St. Louis, MO 63130, USA. Electronic address: rudy@wustl.edu.
Washington University in St. Louis · US

Funding

XRAY CRYSTALLOGRAPHIC STRUCTURE ANALYSIS: PROTEIN SORTINGP41RR001081 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI COHEN, BRUCE E · 1985 to 2011
$17.6M
CARDIAC EXCITATION AND ARRHYTHMIASR01HL049054 · NHLBI · WASHINGTON UNIVERSITY · PI RUDY, YORAM · 1993 to 2017
$5.8M
INVERSE AND FORWARD PROBLEMS IN ELECTROCARDIOGRAPHYR01HL033343 · NHLBI · WASHINGTON UNIVERSITY · PI RUDY, YORAM · 1985 to 2015
$2.9M
NCRR NIH HHS P41 RR001081NHLBI NIH HHS R01 HL033343NHLBI NIH HHS R01-HL033343NHLBI NIH HHS R01 HL049054NHLBI NIH HHS R01-HL049054
6 · The paper itself

Abstract

Ion channels are the "building blocks" of the excitation process in excitable tissues. Despite advances in determining their molecular structure, understanding the relationship between channel protein structure and electrical excitation remains a challenge. The Kv7.1 potassium channel is an important determinant of the cardiac action potential and its adaptation to rate changes. It is subject to beta adrenergic regulation, and many mutations in the channel protein are associated with the arrhythmic long QT syndrome. In this theoretical study, we use a novel computational approach to simulate the conformational changes that Kv7.1 undergoes during activation gating and compute the resulting electrophysiologic function in terms of single-channel and macroscopic currents. We generated all possible conformations of the S4-S5 linker that couples the S3-S4 complex (voltage sensor domain, VSD) to the pore, and all associated conformations of VSD and the pore (S6). Analysis of these conformations revealed that VSD-to-pore mechanical coupling during activation gating involves outward translation of the voltage sensor, accompanied by a translation away from the pore and clockwise twist. These motions cause pore opening by moving the S4-S5 linker upward and away from the pore, providing space for the S6 tails to move away from each other. Single channel records, computed from the simulated motion trajectories during gating, have stochastic properties similar to experimentally recorded traces. Macroscopic current through an ensemble of channels displays two key properties of Kv7.1: an initial delay of activation and fast inactivation. The simulations suggest a molecular mechanism for fast inactivation; a large twist of the VSD following its outward translation results in movement of the base of the S4-S5 linker toward the pore, eliminating open pore conformations to cause inactivation.

Indexed as

Electrophysiological PhenomenaIon Channel GatingModels, MolecularHeartKCNQ1 Potassium ChannelMyocardiumProtein DomainsKCNQ1 Potassium ChannelCardiac arrhythmiaCardiac electrophysiologyComputational biologyIon-channel gatingMechanical coupling

Identifiers

PMID26743208
PMCPMC4955398
OpenAlexW2219456723

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Registered trials

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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.