Abstract
The sodium, potassium-ATPase (NKA) is an important ion pump responsible for the generation of electrochemical gradients across eukaryotic plasma membranes. This protein is a high-value therapeutic target for the treatment of heart failure and several carcinomas. We fused fluorescent proteins to the N and A domains of NKA and investigated conformational changes by quantifying intramolecular FRET. Fluorescence lifetime distribution analysis (FLDA) revealed a decrease in FRET with the addition of 25 mM KCl or 1mM ouabain, suggesting a structure transition to a more open conformation. In addition, the low-FRET conformations show a wider lifetime distribution than high-FRET architectures, which suggests that the open structure has a more dynamic cytoplasmic headpiece than the closed conformation. Ongoing experiments will investigate the voltage dependence of FRET changes and NKA structural heterogeneity.
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