Evidence map›Paper›PMID 22282805›Full record

ArticleScience (New York, N.Y.)2012

Crystal structure of the human K2P TRAAK, a lipid- and mechano-sensitive K+ ion channel.

Stephen G Brohawn, Josefina del Mármol, Roderick MacKinnon

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 252 papers.

0numbers the graph read from it
0cells of the map it votes in
252citing papers in PubMed
20.7field-weighted citation impact, top 1% 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

252 citing papers in PubMed, 421 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Tension TRAAKer: a chemigenetic fluorescent membrane tension reporter.bioRxiv : the preprint server for biology · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Gating mechanism of the two-pore-domain potassium channel THIK1.Nature structural & molecular biology · 2025
    Article
  14. Structure of the human KNature structural & molecular biology · 2025
    Article
  15. Structure of the human TWIK-2 potassium channel and its inhibition by pimozide.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  16. Frontiers in genetics · 2025
    Article
  17. Review
  18. Article
  19. Assessing Protein Surface-Based Scoring for Interpreting Genomic Variants.International journal of molecular sciences · 2024
    Article
  20. Constitutive sodium permeability in aProceedings of the National Academy of Sciences of the United States of America · 2024
    Article

192 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Stephen G BrohawnLaboratory of Molecular Neurobiology and Biophysics and Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA.
Josefina del Mármol
Roderick MacKinnon
Howard Hughes Medical Institute · USRockefeller University · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

TRAAK channels, members of the two-pore domain K(+) (potassium ion) channel family K2P, are expressed almost exclusively in the nervous system and control the resting membrane potential. Their gating is sensitive to polyunsaturated fatty acids, mechanical deformation of the membrane, and temperature changes. Physiologically, these channels appear to control the noxious input threshold for temperature and pressure sensitivity in dorsal root ganglia neurons. We present the crystal structure of human TRAAK at a resolution of 3.8 angstroms. The channel comprises two protomers, each containing two distinct pore domains, which create a two-fold symmetric K(+) channel. The extracellular surface features a helical cap, 35 angstroms tall, that creates a bifurcated pore entryway and accounts for the insensitivity of two-pore domain K(+) channels to inhibitory toxins. Two diagonally opposed gate-forming inner helices form membrane-interacting structures that may underlie this channel's sensitivity to chemical and mechanical properties of the cell membrane.

Indexed as

Amino Acid SequenceAnimalsCell MembraneCHO CellsCricetinaeCrystallizationCrystallography, X-RayHumansHydrophobic and Hydrophilic InteractionsIon Channel GatingLipid BilayersMembrane PotentialsModels, MolecularMolecular Sequence DataPatch-Clamp TechniquesPotassiumKCNK4 protein, humanLipid BilayersPotassiumPotassium Channel BlockersPotassium ChannelsProtein SubunitsRecombinant Proteins

Identifiers

PMID22282805
PMCPMC3329120
OpenAlexW2041345208

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.