Crystal Structure of Na + , K + -ATPase in the Na + -Bound State
pmid: 24051246
Crystal Structure of Na + , K + -ATPase in the Na + -Bound State
Pumping Out Sodium Mammalian cells contain relatively high concentrations of potassium but low concentrations of sodium. This balance is maintained by an ion pump, the Na + , K + –adenosine triphosphatase, in an adenosine triphosphate–driven transport cycle that results in the export of three sodium ions and the import of two potassium ions. Structures of potassium-bound conformations of the pump have been determined. Now, Nyblom et al. (p. 123 , published online 19 September) report on the high-resolution crystal structure of a Na + -bound conformation, which reveals conformational changes associated with Na + binding.
- Stockholm University Sweden
- Aarhus University Denmark
- European Bioinformatics Institute United Kingdom
- Swedish e-Science Research Centre Sweden
- National Research Foundation South Africa
Models, Molecular, Swine, Cell Membrane, Sodium, Crystallography, X-Ray, Protein Structure, Secondary, Protein Structure, Tertiary, Mutation, Animals, Sodium-Potassium-Exchanging ATPase, Protein Binding
Models, Molecular, Swine, Cell Membrane, Sodium, Crystallography, X-Ray, Protein Structure, Secondary, Protein Structure, Tertiary, Mutation, Animals, Sodium-Potassium-Exchanging ATPase, Protein Binding
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