Permeation selectivity was studied in two human potassium channels, Kv
2.1 and Kv1.5, expressed in a mouse cell line. With normal concentrati
ons of potassium and sodium, both channels were highly selective for p
otassium. On removal of potassium, Kv2.1 displayed a large sodium cond
uctance that was inhibited by low concentrations of potassium. The cha
nnel showed a competition mechanism of selectivity similar to that of
calcium channels. In contrast, Kv1.5 displayed a negligible sodium con
ductance on removal of potassium. The observation that structurally si
milar potassium channels show different abilities to conduct sodium pr
ovides a basis for understanding the structural determinants of potass
ium channel selectivity.