Ontology highlight
ABSTRACT:
SUBMITTER: Jakubik J
PROVIDER: S-EPMC5238504 | biostudies-literature | 2017 Jan
REPOSITORIES: biostudies-literature
Jakubík Jan J Randáková Alena A Zimčík Pavel P El-Fakahany Esam E EE Doležal Vladimír V
Scientific reports 20170116
Interaction of orthosteric ligands with extracellular domain was described at several aminergic G protein-coupled receptors, including muscarinic acetylcholine receptors. The orthosteric antagonists quinuclidinyl benzilate (QNB) and N-methylscopolamine (NMS) bind to the binding pocket of the muscarinic acetylcholine receptor formed by transmembrane α-helices. We show that high concentrations of either QNB or NMS slow down dissociation of their radiolabeled species from all five subtypes of musca ...[more]