title: Agonist responses of (R)- and (S)-3-fluoro-γ-aminobutyric acids suggest an enantiomeric fold for GABA binding to GABA(C) receptors.
abstract: The enantiomers of 3F-GABA were evaluated on GABA(C) receptors. Both enantiomers were agonists, with the (R)-enantiomer being an order of magnitude more potent. This result is consistent with a folded binding mode for GABA, a conclusion which suggests a different binding mode to that found in the related but pharmacologically distinct GABA(A) receptors.
authors.affiliation: Faculty of Pharmacy, University of Sydney, NSW, 2006, Australia.
authors.forename: Izumi
authors.initials: I
authors.lastname: Yamamoto
authors.forename: Gildas P
authors.initials: GP
authors.lastname: Deniau
authors.forename: Navnath
authors.initials: N
authors.lastname: Gavande
authors.forename: Mary
authors.initials: M
authors.lastname: Chebib
authors.forename: Graham A R
authors.initials: GA
authors.lastname: Johnston
authors.forename: David
authors.initials: D
authors.lastname: O'Hagan
mesh_terms: D018755:GABA Agonists / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D018079:Receptors, GABA / Q000737:chemistry / Q000378:metabolism*; D013237:Stereoisomerism; D005680:gamma-Aminobutyric Acid / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D018755:GABA Agonists; C087200:GABA-C receptor; D018079:Receptors, GABA; D005680:gamma-Aminobutyric Acid