Full and partial agonists evoke distinct structural changes in opening the muscle acetylcholine receptor channel.

ABSTRACT: The muscle acetylcholine (ACh) receptor transduces a chemical into an electrical signal, but the efficiency of transduction, or efficacy, depends on the particular agonist. It is often presumed that full and partial agonists elicit the same structural changes after occupancy of their binding sites but with differing speed and efficiency. In this study, we tested the alternative hypothesis that full and partial agonists elicit distinct structural changes. To probe structural changes, we substituted cysteines for pairs of residues that are juxtaposed in the three-dimensional structure and recorded agonist-elicited single-channel currents before and after the addition of an oxidizing reagent. The results revealed multiple cysteine pairs for which agonist-elicited channel opening changes after

SUBMITTER: Mukhtasimova N 

PROVIDER: S-EPMC5940249 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature