Partial tertiary structure assignments for the beta-, gamma- and delta-subunits of the acetylcholine receptor on the basis of the hydrophobicity of amino acid sequences and channel location using single group rotation theory.
Four transmembrane segments from each of the beta-, gamma- and delta-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.
D000595:Amino Acid Sequence; D055598:Chemical Phenomena; D002621:Chemistry; D007473:Ion Channels; D011487:Protein Conformation; D011950:Receptors, Cholinergic; D012995:Solubility
D007473:Ion Channels; D011950:Receptors, Cholinergic