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Article

Active conformations of neuronal Na+, K+-ATPase isoforms and a disease-causing mutant.

Nature communications - 29 Jul 2026

Christensen Mads Eskesen, Habeck Michael, Katz Adriana, Fruergaard Marlene Uglebjerg, Peleg Yoav, Pick Uri, Karlish Steven J D, Nissen Poul

Abstract excerpt

Na+,K+-ATPases establish and maintain the vital electrochemical gradients for Na+ and K+ across animal cell membranes. The protein is a ternary complex composed of α, β and FXYD subunits, of which isoforms that fine-tune transport properties are expressed in a tissue-specific fashion. Here we report cryo-EM structures under active ATPase turn-over conditions of the ubiquitously expressed human α1β1FXYD1 and...

Read the complete abstract on PubMed

Topics

Sodium-Potassium-Exchanging ATPase
Humans
Neurons
Sodium
Cryoelectron Microscopy
Mutation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Protein Conformation

Binding Sites

Isoenzymes

Models, Molecular

Animals

Hemiplegia

Source

Open in PubMed Open full text

Identifiers

PMID: 42669691
DOI: 10.1038/s41467-026-75997-4
PMCID: PMC13526833

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 24 Oct 2026.

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