Primary structure and expression of a naturally truncated human P2X ATP receptor subunit from brain and immune system.
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Le KT, Paquet M, Nouel D, Babinski K, Seguela P
Primary structure and expression of a naturally truncated human P2X ATP receptor subunit from brain and immune system.
FEBS Lett. 1997 Nov 24;418(1-2):195-9. doi: 10.1016/s0014-5793(97)01380-x.
- PubMed ID
- 9414125 [ View in PubMed]
- Abstract
A novel member of the ionotropic ATP receptor gene family has been identified in human brain. This 422 amino acid long P2X receptor subunit has 62% sequence identity with rat P2X5. Several characteristic motifs of ATP-gated channels are present in its primary structure, but this P2X5-related subunit displays a single transmembrane domain. Heterologous expression of chimeric subunits containing the C-terminal domain of rat P2X5 leads to the formation of desensitizing functional ATP-gated channels in Xenopus oocytes. The developmentally regulated mRNA, found in two splicing variant forms, is expressed at high levels in brain and immune system.