Abstract
The roles of a glycine-rich region in the cloned P2X 2 receptor/channel were evaluated by site-directed mutagenesis. Responsiveness to ATP was lost when Gly 247 was replaced by alanine. The sensitivity to ATP was reduced when Gly 248 was replaced by alanine, and the responsiveness to ATP was lost when Gly 248 was replaced by valine. The results suggest that the neighboring glycine residues are essential for P2X 2 receptor/channel function.
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