A structural study of the full amino acid sequence of subunits alpha, beta, and delta of the acetylcholine receptor protein.
A Chou and Fasman analysis of the complete amino acid sequence of the alpha, beta and delta subunits of the AChR protein is presented. This shows nine beta strands in comparable loci in all subunits, of which three have (in part) an amphiphilic structure in all subunits (and one has such in 2/3 subunits), giving a total of 12-15 amphiphilic strands. This supports a previous hypothesis that the structure of the ion channel in the AChR protein is a type of beta-barrel or complex of amphiphilic beta-sheets with an extensive hydrophilic surface lining the channel, and an extensive lipophilic surface forming the inside of a beta-sandwich. No other suitable locus for the actual ACh receptor was found on the alpha-subunit other than segment 2-6.
D000595:Amino Acid Sequence; D011950:Receptors, Cholinergic / Q000032:analysis*
D011950:Receptors, Cholinergic