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Partial tertiary structure assignments for the β‐, γ‐ and δ‐ subunits of the acetylcholine receptor on the basis of the hydrophobicity of amino acid sequences and channel location using single group rotation theory
Author(s) -
Kosower Edward M.
Publication year - 1983
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 - 10.1016/0014-5793(82)80613-3
Subject(s) - acetylcholine receptor , chemistry , amino acid , protein subunit , ion channel , transmembrane protein , transmembrane domain , stereochemistry , crystallography , helix (gastropod) , receptor , biophysics , biochemistry , biology , gene , ecology , snail
Four transmembrane segments from each of the β‐, γ‐ and δ‐protein subunits of the acetylcholine receptor (AChR) [Nature (1983) 301, 251–255], [Proc. Natl. Acad. Sci. USA (1983) 80, 1111–1115] have been selected on the basis of single group rotation (SGR) theory [Symp. Structure and Dynamics of Nucleic Acids and Proteins (Sept. 1982) abst. pp.52–53], [Biochem. Biophys. Res. Commun. (1983) 111, 1022–1029] and the hydrophobicity of amino acid sequences. One helix from each subunit is assigned to the AChR ion channel. Criteria for the selection of ion channel elements are outlined.