Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural basis for proton inhibition of the two-pore domain K+ channel TASK-1.

Structure (London, England : 1993) - 2 Jul 2026

Docter Trevor, Lee Nicolas S, Reid Michelle S, Brohawn Stephen G

Abstract excerpt

TASK-1 is a pH-sensitive two-pore domain K+ channel implicated in diseases including pulmonary arterial hypertension (PAH) and developmental delay with sleep apnea (DDSA). Structures of TASK-1 have been captured with an open external gate, but the structural basis for external proton inhibition is incompletely understood. Here, we present a cryo-EM structure of TASK-1 at pH 6.0 and 100 mM K+, revealing a closed...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cryoelectron Microscopy
Share to Hydrogen-Ion Concentration

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ion Channel Gating

Share to Models, Molecular

Share to Mutation

Share to Nerve Tissue Proteins

Share to Potassium Channels, Tandem Pore Domain

Share to Protons

Source

Open in PubMed Open full text

Identifiers

PMID: 42229429
DOI: 10.1016/j.str.2026.05.002
PMCID: PMC13317458

Genes

PAH

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis for proton inhibition of the two-pore domain K+ channel TASK-1.PMID 42229429Read ↗

Structural basis for proton inhibition of the two-pore domain K <sup>+</sup> channel TASK-1Semantic proximity Read ↗

Structures of TASK-1 and TASK-3 K2P channels provide insight into their gating and dysfunction in diseaseSemantic proximity Read ↗

Fine-tuning pH sensor H98 by remote essential residues in the hydrogen-bond network of mTASK-3.Semantic proximity Read ↗

Determinants of pH sensing in the two-pore domain K(+) channels TASK-1 and -2.Semantic proximity Read ↗

Structural and molecular insight into the pH-induced low-permeability of the voltage-gated potassium channel Kv1.2 through dewetting of the water cavity.Semantic proximity Read ↗

Ion occupancy of the selectivity filter controls opening of a cytoplasmic gate in the K2P channel TALK-2.Semantic proximity Read ↗

A unique lower X-gate in TASK channels traps inhibitors within the vestibuleSemantic proximity Read ↗

A lower X-gate in TASK channels traps inhibitors within the vestibule.Semantic proximity Read ↗

A flexible GAS belt responds to pore mutations changing the ion selectivity of proton-gated channels.Semantic proximity Read ↗

Molecular basis of proton-sensing by G protein-coupled receptorsSemantic proximity Read ↗

Deep mutational scan of the pore of the cold-sensing TRPM8 channelSemantic proximity Read ↗

Hydrophobic pore gates regulate ion permeation in polycystic kidney disease 2 and 2L1 channels.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.