Abstract：
:The nicotinic acetylcholine receptor (AChR) from the electroplax of the ray Torpedo californica is composed of five subunits present in a molar stoichiometry of alpha 2 beta gamma delta (refs 1-3) and contains both the binding site for the neurotransmitter and the cation gating unit (reviewed in refs 4-6). We have recently elucidated the complete primary structures of the alpha-, beta- and delta-subunit precursors of the T. californica AChR by cloning and sequencing cDNAs for these polypeptides. Here, we report the whole primary structure of the gamma-subunit precursor of the AChR deduced from the nucleotide sequence of the cloned cDNA. Comparison of the amino acid sequences of the four subunits reveals marked homology among them. The close resemblance among the hydrophilicity profiles and predicted secondary structures of all the subunits suggests that these polypeptides are oriented in a pseudosymmetric fashion across the membrane. Each subunit contains four putative transmembrane segments that may be involved in the ionic channel. The transmembrane topology of the subunit molecules has also been inferred.
journal_name
Naturejournal_title
Natureauthors
Noda M,Takahashi H,Tanabe T,Toyosato M,Kikyotani S,Furutani Y,Hirose T,Takashima H,Inayama S,Miyata T,Numa Sdoi
10.1038/302528a0subject
Has Abstractpub_date
1983-04-07 00:00:00pages
528-32issue
5908eissn
0028-0836issn
1476-4687journal_volume
302pub_type
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