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Molecular Biophysics
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- ArticleOpen Access
Altered allostery of the left flipper domain underlies the weak ATP response of rat P2X5 receptors
Journal of Biological ChemistryVol. 294Issue 51p19589–19603Published online: November 14, 2019- Liang-Fei Sun
- Yan Liu
- Jin Wang
- Li-Dong Huang
- Yang Yang
- Xiao-Yang Cheng
- and others
Cited in Scopus: 7Although the extracellular ATP-gated cation channel purinergic receptor P2X5 is widely expressed in heart, skeletal muscle, and immune and nervous systems in mammals, little is known about its functions and channel-gating activities. This lack of knowledge is due to P2X5’s weak ATP responses in several mammalian species, such as humans, rats, and mice. WT human P2X5 (hP2X5Δ328–349) does not respond to ATP, whereas a full-length variant, hP2X5 (hP2X5-FL), containing exon 10 encoding the second hP2X5 transmembrane domain (TM2), does.