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FEBS Lett. 1997 Nov 24;418(1-2):195-9.

Primary structure and expression of a naturally truncated human P2X ATP receptor subunit from brain and immune system.

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Cell Biology of Excitable Tissue Group, Montreal Neurological Institute, McGill University, Que., Canada.


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.

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