Enantiomeric barbiturates bind distinct inter- and intrasubunit binding sites in a nicotinic acetylcholine receptor (nAChR).

ABSTRACT: Nicotinic acetylcholine receptors (nAChRs) and γ-aminobutyric acid type A receptors (GABA_ARs) are members of the pentameric ligand-gated ion channel superfamily. Drugs acting as positive allosteric modulators of muscle-type α₂βγδ nAChRs, of use in treatment of neuromuscular disorders, have been hard to identify. However, identification of nAChR allosteric modulator binding sites has been facilitated by using drugs developed as photoreactive GABA_AR modulators. Recently, R-1-methyl-5-allyl-5-(m-trifluoromethyl-diazirinylphenyl) barbituric acid (R-mTFD-MPAB), an anesthetic and GABA_AR potentiator, has been shown to inhibit Torpedo α₂βγδ nAChRs, binding in the ion channel and to a γ⁺-α^- subu

SUBMITTER: Yu Z 

PROVIDER: S-EPMC5655505 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature