Evidence map›Paper›PMID 16983069›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Electrostatic interactions in the channel cavity as an important determinant of potassium channel selectivity.

Delphine Bichet, Michael Grabe, Yuh Nung Jan, Lily Yeh Jan

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. 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
2.7field-weighted citation impact, top 10% 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, 46 citations in OpenAlex.

  1. Understanding Ion Channel Gating Mechanisms by Molecular Dynamics Simulations.Advances in experimental medicine and biology · 2026
    Review
  2. Preorganized Electric Fields in Voltage-Gated Sodium Channels.Chembiochem : a European journal of chemical biology · 2025
    Article
  3. Article
  4. TOK channels use the two gates in classical KFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
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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

4 authors at 2 institutions in 1 country.

Delphine BichetDepartments of Physiology and Biochemistry and Howard Hughes Medical Institute, University of California, San Francisco, CA 94143.
Michael Grabe
Yuh Nung Jan
Lily Yeh Jan
Howard Hughes Medical Institute · USUniversity of California, San Francisco · US

Funding

Genetic Studies of the SynapseR01MH065334 · NIMH · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI JAN, LILY Y · 2001 to 2020
$3.8M
Genetic Studies of the SynapseR37MH065334 · NIMH · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI JAN, LILY Y · 2006 to 2015
$3.8M
NIMH NIH HHS MH 065334NIMH NIH HHS R01 MH065334NIMH NIH HHS R37 MH065334
6 · The paper itself

Abstract

Potassium channels are membrane proteins that allow the passage of potassium ions at near diffusion rates while severely limiting the flux of the slightly smaller sodium ions. Although studies thus far have focused on the narrowest part of the channel, known as the selectivity filter, channels are long pores with multiple ions that traverse the selectivity filter, the water-filled central cavity, and the rest of the pore formed by cytoplasmic domains. Here, we present experimental analyses on Kir3.2 (GIRK2), a G protein-activated inwardly rectifying potassium (Kir) channel, showing that a negative charge introduced at a pore-facing position in the cavity (N184) below the selectivity filter restores both K(+) selectivity and inward rectification properties to the nonselective S177W mutant channel. Molecular modeling demonstrates that the negative residue has no effect on the geometry of the selectivity filter, suggesting that it has a local effect on the cavity ion. Moreover, restoration of selectivity does not depend on the exact location of the charge in the central cavity as long as this residue faces the pore, where it is in close contact with permeant ions. Our results indicate that interactions between permeant ions and the channel cavity can influence ion selectivity and channel block by means of an electrostatic effect.

Indexed as

Ion Channel GatingAmino AcidsAnimalsCell Membrane PermeabilityG Protein-Coupled Inwardly-Rectifying Potassium ChannelsModels, MolecularMutationOocytesProtein Structure, SecondaryStatic ElectricityStructure-Activity RelationshipXenopus laevisAmino AcidsG Protein-Coupled Inwardly-Rectifying Potassium Channels

Identifiers

PMID16983069
PMCPMC1570129
OpenAlexW2156071488

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.