The Conformation of ATP within the Na,K-ATPase Nucleotide Site: A Statistically Constrained Analysis of REDOR Solid-State NMR Data

The Conformation of ATP within the Na,K-ATPase Nucleotide Site: A Statistically Constrained Analysis of REDOR Solid-State NMR Data

Simplification through statistics: The conformation of adenosine triphosphate (ATP) bound to the high‐affinity nucleotide site of Na,K‐ATPase in its native membrane (see picture) can be determined by REDOR solid‐state NMR measurements. The structural analysis of ligands may be improved dramatically...

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Veröffentlicht in:Angewandte Chemie International Edition 2011-07, Vol.50 (31), p.7041-7044
Hauptverfasser: Middleton, David A., Hughes, Eleri, Esmann, Mikael
Format: Artikel
Sprache:eng
Schlagworte:
adenosine triphosphate
Adenosine Triphosphate - chemistry
Adenosine Triphosphate - metabolism
Animals
Binding Sites
conformation analysis
Models, Molecular
Molecular Conformation
NMR spectroscopy
Nuclear Magnetic Resonance, Biomolecular - methods
nucleotide ligands
Sodium-Potassium-Exchanging ATPase - chemistry
Sodium-Potassium-Exchanging ATPase - metabolism
Swine
torsional angles
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Zusammenfassung:Simplification through statistics: The conformation of adenosine triphosphate (ATP) bound to the high‐affinity nucleotide site of Na,K‐ATPase in its native membrane (see picture) can be determined by REDOR solid‐state NMR measurements. The structural analysis of ligands may be improved dramatically by considering their conformational preferences based on the statistical analysis of a limited number of 31P–13C distances.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201100736