Abstract
In the closed structure of the P2X cation channel, three α-helical transmembrane domains cross the membrane obliquely: in rat P2X2 receptors, these intersect at Thr339. Replacing Thr339 by lysine in one, two or three subunits progressively increased chloride permeability and reduced unitary conductance. This implies that the closed-open transition involves a symmetrical separation of the three subunits, and that Thr339 from each contributes symmetrically to the open channel permeation pathway.
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