Evidence map›Paper›PMID 21933962›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Protein interactions central to stabilizing the K+ channel selectivity filter in a four-sited configuration for selective K+ permeation.

David B Sauer, Weizhong Zeng, Srinivasan Raghunathan, Youxing Jiang

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Ion and water permeation through claudin-10b and claudin-15 paracellular channels.Computational and structural biotechnology journal · 2024
    Article
  5. Article
  6. Article
  7. Structural Basis for pH-gating of the KNature communications · 2022
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Exploring the Viral Channel KcvThe Journal of membrane biology · 2018
    Article
  14. Article
  15. Article
  16. Ion channels and ion selectivity.Essays in biochemistry · 2017
    Review
  17. Tuning the ion selectivity of two-pore channels.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  18. Article
  19. Role of protein dynamics in ion selectivity and allosteric coupling in the NaK channel.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  20. Review
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.

David B SauerDepartment of Physiology, and Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390-9040, USA.
Weizhong Zeng
Srinivasan Raghunathan
Youxing Jiang

Funding

Structural mechanisms of ion selectivity and gating in tetrameric cation channelsR01GM079179 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI JIANG, YOUXING · 2007 to 2019
$3.5M
Molecular Biophysics Predoctoral Training ProgramT32GM008297 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI CHOOK, YUH MIN · 1989 to 2018
$2.4M
Howard Hughes Medical InstituteNIGMS NIH HHS GM079179NIGMS NIH HHS R01 GM079179NIGMS NIH HHS T32 GM008297NIGMS NIH HHS T32GM008297
6 · The paper itself

Abstract

The structural and functional conversion of the nonselective NaK channel to a K(+) selective channel (NaK2K) allows us to identify two key residues, Tyr and Asp in the filter sequence of TVGYGD, that participate in interactions central to stabilizing the K(+) channel selectivity filter. By using protein crystallography and channel electrophysiology, we demonstrate that the K(+) channel filter exists as an energetically strained structure and requires these key protein interactions working in concert to hold the filter in the precisely defined four-sited configuration that is essential for selective K(+) permeation. Disruption of either interaction, as tested on both the NaK2K and eukaryotic K(v)1.6 channels, can reduce or completely abolish K(+) selectivity and in some cases may also lead to channel inactivation due to conformational changes at the filter. Additionally, on the scaffold of NaK we recapitulate the protein interactions found in the filter of the Kir channel family, which uses a distinct interaction network to achieve similar stabilization of the filter.

Indexed as

Models, MolecularProtein ConformationAmino Acid MotifsCrystallographyElectrophysiologyPotassiumSodium-Potassium-Exchanging ATPasePotassiumSodium-Potassium-Exchanging ATPase

Identifiers

PMID21933962
PMCPMC3189067

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.