Tertiary Structure of the Nicotinic Acetylcholine Receptor Probed by Photolabeling and Protein Chemistry
The nicotinic Ach-receptor in vertebrates consists of four subunits assembled into an heterologous α2βγδ pentamer. The cDNAs coding for the constitutive four chains of the Ach-receptor have been cloned and sequenced in T.californica (Ballivet et al., 1982, Noda et al., 1982, 1983a,b, Claudio et al., 1983), in T. marmorata (for the a chain: Giraudat et al., 1982, Sumikawa et al., 1982, Devillers-Thiéry et al., 1983) and in several vertebrate species, including humans (ref. in Kubo et al., 1985 and Boulter et al., 1986). The four subunits display striking homologies in sequence and similar hydrophobicity profiles suggesting an organization of the molecule into a transmembrane bundle of subunits with a 5-fold axis of quasi-symmetry perpendicular to the plane of the membrane (ref. in Bon et al., 1984, Brisson and Unwin 1985, McCarthy et al., 1986).
KeywordsTryptic Peptide Cyanogen Bromide High Affinity Site Hydrophobic Segment Agonist Binding Site
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