[HTML][HTML] Primary structure and expression of a naturally truncated human P2X ATP receptor subunit from brain and immune system
KT Lê, M Paquet, D Nouel, K Babinski, P Séguéla - FEBS letters, 1997 - Elsevier
KT Lê, M Paquet, D Nouel, K Babinski, P Séguéla
FEBS letters, 1997•ElsevierA 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 …
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 …
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.
Elsevier
