Structural insights into the binding of cardiac glycosides to the digitalis receptor revealed by solid-state NMR.

Journal article

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 ...

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Authors: Middleton, D; Rankin, S; Esmann, M; Watts, A

• Publication status: Published
• Journal: Proceedings of the National Academy of Sciences of the United States of America
• Volume: 97
• Issue: 25
• Pages: 13602-13607
• Publication date: 2000-12-01
• DOI: 10.1073/pnas.250471997
• EISSN: 1091-6490
• ISSN: 0027-8424
• Language: English
• Keywords: Carbohydrate Conformation; Nuclear Magnetic Resonance, Biomolecular; Cardiac Glycosides; Sodium-Potassium-Exchanging ATPase; Protein Binding