Figure 1. Structure of the Na/K pump α subunit and representation of its transport cycle. (A) Angled extracellular view of Na,K-ATPase α-subunit structure (Morth et al., 2007) indicating locations (Xenopus numbering) of mutations introduced here in Xenopus Na,K-ATPase α1 subunits to confer ouabain resistance, C113Y (red) or Q120R/N131D (green), and C-terminal truncation, ΔYY or ΔKESYY (blue). (B) Cartoon of an alternating-gate representation (Artigas and Gadsby, 2003) of the Post-Albers transport cycle of the Na/K pump, indicating E1 states with the extracellular-side gate (red) closed and cytoplasmic access to ion-binding sites and E2 states with the cytoplasmic-side gate (blue) closed and extracellular access to ion-binding sites. The dashed box encloses the phosphorylated pump conformations linked in a voltage-dependent equilibrium in the presence of saturating Nai and ATP and of Nao but in the absence of Ko.
Figure 1.

Structure of the Na/K pump α subunit and representation of its transport cycle. (A) Angled extracellular view of Na,K-ATPase α-subunit structure (Morth et al., 2007) indicating locations (Xenopus numbering) of mutations introduced here in Xenopus Na,K-ATPase α1 subunits to confer ouabain resistance, C113Y (red) or Q120R/N131D (green), and C-terminal truncation, ΔYY or ΔKESYY (blue). (B) Cartoon of an alternating-gate representation (Artigas and Gadsby, 2003) of the Post-Albers transport cycle of the Na/K pump, indicating E1 states with the extracellular-side gate (red) closed and cytoplasmic access to ion-binding sites and E2 states with the cytoplasmic-side gate (blue) closed and extracellular access to ion-binding sites. The dashed box encloses the phosphorylated pump conformations linked in a voltage-dependent equilibrium in the presence of saturating Nai and ATP and of Nao but in the absence of Ko.

This Feature Is Available To Subscribers Only

or Create an Account

Close Modal
Close Modal