Structural features of the nicotinic acetylcholine receptor revealed by antibodies to synthetic peptides.

Antibodies were raised to the amino- and carboxy-terminal decapeptides of Torpedo californica acetylcholine receptor. Structural studies of the native receptor using the antipeptide antibodies as probes proved the existence of the carboxy terminal sequence in the alpha subunit predicted from its cDNA sequence and supported structural models of the native receptor that place the carboxy termini on the intracellular side. The amino termini of the subunits were not accessible on the surface of native receptor.