Structural modelling of Na⁺,K⁺-ATPase α3 mutations.

<p>(A) Na⁺,K⁺-ATPase α3 wild-type (left), the I810S mutant (AHC; centre) and the I810N mutant (<i>Myshkin</i>; right). (B) Na⁺,K⁺-ATPase α3 wild-type (left), the I274N mutant (AHC; centre) and the I274T mutant (RDP; right). Side chain contact between Δ272 and Δ274 at the cytoplasmic end of the K⁺ pore is shown in yellow for the wild-type protein and the I274T mutant, but this contact is lost in the I274N mutant. (C) Na⁺,K⁺-ATPase α3 wild-type (left), the D801N mutant (AHC; centre) and D801Y mutant (RDP; right). In the D801N mutant, the electrostatic interaction at Δ801 with both K⁺ ions is lost due to replacement of terminal oxygen with nitrogen, resulting in the obstruction of the K⁺ pore, likely to markedly affect conductance rates through the pore, while the interaction of K⁺2 with E776 is maintained. In the D801Y mutant, there is a predicted loss of interaction of K⁺2 with E776. (D) Na⁺,K⁺-ATPase α3 wild-type (left), the D923Y mutant (AHC; centre) and the D923N mutant (RDP; right).