Na<sup>+</sup>,K<sup>+</sup>-ATPase with Disrupted Na<sup>+</sup> Binding Sites I and III Binds Na<sup>+</sup> with Increased Affinity at Site II and Undergoes Na<sup>+</sup>-Activated Phosphorylation with ATP

Na<sup>+</sup>,K<sup>+</sup>-ATPase with Disrupted Na<sup>+</sup> Binding Sites I and III Binds Na<sup>+</sup> with Increased Affinity at Site II and Undergoes Na<sup>+</sup>-Activated Phosphorylation with ATP

Na<sup>+</sup>,K<sup>+</sup>-ATPase actively extrudes three cytoplasmic Na<sup>+</sup> ions in exchange for two extracellular K<sup>+</sup> ions for each ATP hydrolyzed. The atomic structure with bound Na<sup>+</sup> identifies three Na<...

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Bibliographic Details
Main Authors: Hang N. Nielsen, Rikke Holm, Ryan Sweazey, Jens Peter Andersen, Pablo Artigas, Bente Vilsen
Format: Article
Language:English
Published: MDPI AG 2024-01-01
Series:Biomolecules
Subjects:
Na<sup>+</sup>,K<sup>+</sup>-pump
Na<sup>+</sup> site
K<sup>+</sup> site
Na<sup>+</sup> affinity
K<sup>+</sup> affinity
P-type ATPase
Online Access:https://www.mdpi.com/2218-273X/14/1/135

Internet

https://www.mdpi.com/2218-273X/14/1/135

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