ArticleProceedings of the National Academy of Sciences of the United States of America2000
Structural insights into the binding of cardiac glycosides to the digitalis receptor revealed by solid-state NMR.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 60 citations in OpenAlex.
- Article
- Probing the stereoselectivity of OleD-catalyzed glycosylation of cardiotonic steroids.RSC advances · 2018Article
- Novel stereoselective bufadienolides reveal new insights into the requirements for Na(+), K(+)-ATPase inhibition by cardiotonic steroids.Scientific reports · 2016Article
- A structural rearrangement of the Na+/K+-ATPase traps ouabain within the external ion permeation pathway.Journal of molecular biology · 2015Article
- Cardiac glycoside activities link Na(+)/K(+) ATPase ion-transport to breast cancer cell migration via correlative SAR.ACS chemical biology · 2015Article
- Ouabain binding site in a functioning Na+/K+ ATPase.The Journal of biological chemistry · 2011Article
- The non-gastric H,K-ATPase as a tool to study the ouabain-binding site in Na,K-ATPase.Pflugers Archiv : European journal of physiology · 2009Article
- Ouabain affinity determining residues lie close to the Na/K pump ion pathway.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Large diameter of palytoxin-induced Na/K pump channels and modulation of palytoxin interaction by Na/K pump ligands.The Journal of general physiology · 2004Article
- High resolution 13C NMR spectra on oriented lipid bilayers: from quantifying the various sources of line broadening to performing 2D experiments with 0.2-0.3 ppm resolution in the carbon dimension.Journal of biomolecular NMR · 2002Article
- Towards high-resolution solid-state NMR on large uniformly 15N- and [13C,15N]-labeled membrane proteins in oriented lipid bilayers.Journal of biomolecular NMR · 2002Article
- Structural similarities of Na,K-ATPase and SERCA, the Ca(2+)-ATPase of the sarcoplasmic reticulum.The Biochemical journal · 2001Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several biologically active derivatives of the cardiotonic steroid ouabain have been made containing NMR isotopes ((13)C, (2)H, and (19)F) in the rhamnose sugar and steroid moieties, and examined at the digitalis receptor site of renal Na(+)/K(+)-ATPase by a combination of solid-state NMR methods. Deuterium NMR spectra of (2)H-labeled inhibitors revealed that the sugar group was only loosely associated with the binding site, whereas the steroid group was more constrained, probably because of hydrogen bonding to residues around the K(+)-channel region. Crosspolarization magic-angle spinning NMR showed that chemical shifts of inhibitors (13)C-labeled in the sugar group moved downfield by 0.5 ppm after binding to the digitalis site, suggesting that the sugar was close to aromatic side groups. A (19)F, (13)C- rotational-echo double-resonance NMR strategy was used to determine the structure of an inhibitor in the digitalis receptor site, and it showed that the ouabain derivatives adopt a conformation in which the sugar extends out of the plane of the steroid ring system. The combined structural and dynamic information favors a model for inhibition in which the ouabain analogues lie across the surface of the Na(+)/K(+)-ATPase alpha-subunit with the sugar group facing away from the surface of the membrane but free to move into contact with one or more aromatic residues.
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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.