Neighboring glycine residues are essential for P2X2 receptor/channel function.
The roles of a glycine-rich region in the cloned P2X2 receptor/channel were evaluated by site-directed mutagenesis. Responsiveness to ATP was lost when Gly247 was replaced by alanine. The sensitivity to ATP was reduced when Gly248 was replaced by alanine, and the responsiveness to ATP was lost when Gly248 was replaced by valine. The results suggest that the neighboring glycine residues are essential for P2X2 receptor/channel function.
Nakazawa
K
K
Division of Pharmacology, National Institute of Health Sciences, Setagaya, Tokyo, Japan. nakazawa@nihs.go.jp
Ohno
Y
Y
D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000409:Alanine / Q000737:chemistry*; D000818:Animals; D005998:Glycine / Q000737:chemistry*; D009154:Mutation; D009865:Oocytes / Q000502:physiology; D018048:Receptors, Purinergic P2 / Q000737:chemistry* / Q000502:physiology; D058476:Receptors, Purinergic P2X2; D014981:Xenopus / Q000502:physiology
D018048:Receptors, Purinergic P2; D058476:Receptors, Purinergic P2X2; D000255:Adenosine Triphosphate; D000409:Alanine; D005998:Glycine