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Primary structure and expression of a naturally truncated human P2X ATP receptor subunit from brain and immune system
Author(s) -
Lê Khanh-Tuoc,
Paquet Michel,
Nouel Dominique,
Babinski Kazimierz,
Séguéla Philippe
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01380-x
Subject(s) - protein subunit , xenopus , alternative splicing , rna splicing , microbiology and biotechnology , biology , transmembrane domain , receptor , heterologous expression , messenger rna , gene , genetics , recombinant dna , rna
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 P2X 5 . Several characteristic motifs of ATP‐gated channels are present in its primary structure, but this P2X 5 ‐related subunit displays a single transmembrane domain. Heterologous expression of chimeric subunits containing the C‐terminal domain of rat P2X 5 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.