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Letters to Nature
Nature 302, 528 - 532 (07 April 1983); doi:10.1038/302528a0

Structural homology of Torpedo californica acetylcholine receptor subunits

Masaharu Noda*, Hideo Takahashi*, Tsutomu Tanabe*, Mitsuyoshi Toyosato*, Sho Kikyotani*, Yasuji Furutani*, Tadaaki Hirose, Hideaki Takashima, Seiichi Inayama, Takashi Miyata & Shosaku Numa*

*Department of Medical Chemistry, Kyoto University Faculty of Medicine, Kyoto 606, Japan
Pharmaceutical Institute, Keio University School of Medicine, Tokyo 160, Japan
Department of Biology, Kyushu University Faculty of Science, Fukuoka 812, Japan

The nicotinic acetylcholine receptor (AChR) from the electroplax of the ray Torpedo californica is composed of five subunits present in a molar stoichiometry of α 2 βγδ (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 α-, β- and δ-subunit precursors of the T. californica AChR by cloning and sequencing cDNAs for these polypeptides7,8. Here, we report the whole primary structure of the γ-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.

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