Evidence map›Paper›PMID 19564427›Full record

ArticleThe Journal of general physiology2009

A structural model for K2P potassium channels based on 23 pairs of interacting sites and continuum electrostatics.

Astrid Kollewe, Albert Y Lau, Ashley Sullivan, Benoît Roux, Steve A N Goldstein

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2009. 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
3.2field-weighted citation impact, top 7% 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, 42 citations in OpenAlex.

  1. The Pharmacology of Two-Pore Domain Potassium Channels.Handbook of experimental pharmacology · 2021
    Article
  2. Article
  3. TOK channels use the two gates in classical KFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
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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.

Astrid KolleweInstitute for Molecular Pediatric Sciences, Department of Pediatrics, The University of Chicago, Pritzker School of Medicine, Chicago, IL 60637, USA.
Albert Y Lau
Ashley Sullivan
Benoît Roux
Steve A N Goldstein
Institute for Molecular Medicine · USUniversity of Chicago · US

Funding

Computational Studies of Ion Channels - Resubmission 01R01GM062342 · NIGMS · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI ROUX, BENOIT · 2001 to 2022
$8.7M
OAT--A NOVEL CARDIAC POTASSIUM CHANNEL WITH 2 P DOMAINSR01HL061657 · NHLBI · YALE UNIVERSITY · PI GOLDSTEIN, STEVE A N · 1999 to 2008
$3.6M
NHLBI NIH HHS R01 HL061657NHLBI NIH HHS R01HL61657NIGMS NIH HHS R01 GM062342NIGMS NIH HHS R01GM62342
6 · The paper itself

Abstract

K(2P)Ø, the two-pore domain potassium background channel that determines cardiac rhythm in Drosophila melanogaster, and its homologues that establish excitable membrane activity in mammals are of unknown structure. K(2P) subunits have two pore domains flanked by transmembrane (TM) spans: TM1-P1-TM2-TM3-P2-TM4. To establish spatial relationships in K(2P)Ø, we identified pairs of sites that display electrostatic compensation. Channels silenced by the addition of a charge in pore loop 1 (P1) or P2 were restored to function by countercharges at specific second sites. A three-dimensional homology model was determined using the crystal structure of K(V)1.2, effects of K(2P)Ø mutations to establish alignment, and compensatory charge-charge pairs. The model was refined and validated by continuum electrostatic free energy calculations and covalent linkage of introduced cysteines. K(2P) channels use two subunits arranged so that the P1 and P2 loops contribute to one pore, identical P loops face each other diagonally across the pore, and the channel complex has bilateral symmetry with a fourfold symmetric selectivity filter.

Indexed as

Models, ChemicalModels, MolecularAmino Acid SequenceBinding SitesComputer SimulationDrosophila ProteinsMolecular Sequence DataPotassium ChannelsProtein BindingProtein ConformationStatic ElectricityDrosophila ProteinsPotassium Channels

Identifiers

PMID19564427
PMCPMC2712977
OpenAlexW2145723908

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.