Open AccessComplete mRNA coding sequence of the acetylcholine binding alpha-subunit of Torpedo marmorata acetylcholine receptor: a model for the transmembrane organization of the polypeptide chain.
Author(s) -
Anne DevillersThiéry,
Jérôme Giraudat,
Martine Bentaboulet,
JeanPierre Changeux
Publication year - 1983
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.80.7.2067
Subject(s) - torpedo , complementary dna , acetylcholine receptor , biology , interleukin 5 receptor alpha subunit , peptide sequence , interleukin 10 receptor, alpha subunit , transmembrane protein , microbiology and biotechnology , g alpha subunit , untranslated region , coding region , nucleic acid sequence , transmembrane domain , clone (java method) , protein subunit , messenger rna , alpha (finance) , amino acid , biochemistry , receptor , gene , medicine , construct validity , nursing , patient satisfaction
A 1,350-base-pair-long cDNA clone, named p alpha-2, was isolated by hybridization to the previously characterized clone p alpha-1 and found to be specific for the alpha-subunit of the Torpedo marmorata acetylcholine receptor. The nucleotide sequences of both cDNA inserts were analyzed and the sequence of the complete coding region and part of the 5' and 3' untranslated regions of the alpha-chain mRNA was determined. The complete amino acid sequence of the alpha-chain precursor is presented and used to develop a model for the transmembrane organization of the polypeptide.