ArticleJournal of molecular biology2015
A structural rearrangement of the Na+/K+-ATPase traps ouabain within the external ion permeation pathway.
Article in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- FXYD proteins and sodium pump regulatory mechanisms.The Journal of general physiology · 2021Review
- Displacement of the NaProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Expression of α2-Na/K-ATPase in C57BL/6J Mice Inner Ear and Its Relationship with Age-related Hearing Loss.Current medical science · 2021Article
- Retinoschisin and Cardiac Glycoside Crosstalk at the Retinal Na/K-ATPase.Investigative ophthalmology & visual science · 2020Article
- Nav channel binder containing a specific conjugation-site based on a low toxicity β-scorpion toxin.Scientific reports · 2017Article
- Nanofibrous scaffolds for the guidance of stem cell-derived neurons for auditory nerve regeneration.PloS one · 2017Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
With the use of the energy of ATP hydrolysis, the Na+/K+-ATPase is able to transport across the cell membrane Na+ and K+ against their electrochemical gradients. The enzyme is strongly inhibited by ouabain and its derivatives, some that are therapeutically used for patients with heart failure (cardiotonic steroids). Using lanthanide resonance energy transfer, we trace here the conformational changes occurring on the external side of functional Na+/K+-ATPases induced by the binding of ouabain. Changes in donor/acceptor pair distances are mainly observed within the α subunit of the enzyme. To derive a structural model matching the experimental lanthanide resonance energy transfer distances measured with bound ouabain, we carried out molecular dynamics simulations with energy restraints applied simultaneously using a novel methodology with multiple non-interacting fragments. The restrained simulation, initiated from the X-ray structure of the E2(2K+) state, became strikingly similar to the X-ray structure of the sodium-bound state. The final model shows that ouabain is trapped within the external ion permeation pathway of the pump.
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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.