Cation and cardiac glycoside binding sites of the Na,K-ATPase

Abstract

From the structural data obtained by systematically altering residues of the Na,K-ATPase, we are beginning to understand portions of how this active cation transporter couples hydrolysis of ATP with the vectorial movement of cations against their ionic gradients. In addition, the inhibitory action of cardiac glycosides and their interaction sites on the protein has focused our attentions on a catalytic core of the protein involving the H5-H6 transmembrane segment. In future investigations, both the ATP and the Na+ sites of the Na,K-ATPase must be uncovered to refine the structural picture of this complex transporter.