ArticleThe Journal of biological chemistry2011
Ouabain binding site in a functioning Na+/K+ ATPase.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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Who cites it
31 citing papers in PubMed, 57 citations in OpenAlex.
- Exploring the Mechanism of NabioRxiv : the preprint server for biology · 2026Article
- Sodium disrupts mitochondrial energy metabolism to execute NECSO.Nature communications · 2025Article
- Magnetic Targeting of AAV Gene Therapy for Inner Ear Following Systemic Delivery: Preliminary Findings and Transduction Pattern in Rat Cochlea.Journal of the Association for Research in Otolaryngology : JARO · 2025Article
- Central nervous system mechanisms of salt-sensitive hypertension.Physiological reviews · 2025Review
- Simplified Method for Kinetic and Thermodynamic Screening of Cardiotonic Steroids through the KMolecular pharmacology · 2024Article
- The host-targeting compound peruvoside has a broad-spectrum antiviral activity against positive-sense RNA viruses.Acta pharmaceutica Sinica. B · 2023Article
- Testis-Specific Isoform of NaInternational journal of molecular sciences · 2022Review
- Intracellular Calcium and Sodium Modulation of Self-Assembled Neocartilage Using Costal Chondrocytes.Tissue engineering. Part A · 2022Article
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- A NaFrontiers in cell and developmental biology · 2021Article
- Lyn regulates creatine uptake in an imatinib-resistant CML cell line.Biochimica et biophysica acta. General subjects · 2020Article
- Protein kinase C mediates juvenile hormone-dependent phosphorylation of NaThe Journal of biological chemistry · 2018Article
- Molecular determination of claudin-15 organization and channel selectivity.The Journal of general physiology · 2018Article
- Apical Cell-Cell Adhesions Reconcile Symmetry and Asymmetry in Zebrafish Neurulation.iScience · 2018Article
- Luminescence resonance energy transfer between genetically encoded donor and acceptor for protein-protein interaction studies in the molecular chaperone HSP70/HSP90 complexes.Scientific reports · 2018Article
- The Administration of Levocabastine, a NTS2 Receptor Antagonist, Modifies Na(+), K(+)-ATPase Properties.Neurochemical research · 2016Article
- P2C-Type ATPases and Their Regulation.Molecular neurobiology · 2016Review
- Specialized Functional Diversity and Interactions of the Na,K-ATPase.Frontiers in physiology · 2016Review
- Mechanism of ammonia excretion in the freshwater leech Nephelopsis obscura: characterization of a primitive Rh protein and effects of high environmental ammonia.American journal of physiology. Regulatory, integrative and comparative physiology · 2015Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
Abstract
The Na(+)/K(+) ATPase is an almost ubiquitous integral membrane protein within the animal kingdom. It is also the selective target for cardiotonic derivatives, widely prescribed inhibitors for patients with heart failure. Functional studies revealed that ouabain-sensitive residues distributed widely throughout the primary sequence of the protein. Recently, structural work has brought some consensus to the functional observations. Here, we use a spectroscopic approach to estimate distances between a fluorescent ouabain and a lanthanide binding tag (LBT), which was introduced at five different positions in the Na(+)/K(+) ATPase sequence. These five normally functional LBT-Na(+)/K(+) ATPase constructs were expressed in the cell membrane of Xenopus laevis oocytes, operating under physiological internal and external ion conditions. The spectroscopic data suggest two mutually exclusive distances between the LBT and the fluorescent ouabain. From the estimated distances and using homology models of the LBT-Na(+)/K(+) ATPase constructs, approximate ouabain positions could be determined. Our results suggest that ouabain binds at two sites along the ion permeation pathway of the Na(+)/K(+) ATPase. The external site (low apparent affinity) occupies the same region as previous structural findings. The high apparent affinity site is, however, slightly deeper toward the intracellular end of the protein. Interestingly, in both cases the lactone ring faces outward. We propose a sequential ouabain binding mechanism that is consistent with all functional and structural studies.
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Registered trials
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.