Benson JA Löw K Keist R Mohler H Rudolph U 1998 Amino acids in the alpha- and gamma-subunits contribute to the benzodiazepine binding site of GABA(A)-receptors. We show that the mutation of a conserved histidine residue in the N-terminal extracellular segment (alpha1H101R, alpha2H101R, alpha3H126R, and alpha5H105R) results not only in diazepam-insensitivity of the respective alphaxbeta2,3gamma2-receptors but also in an increased potentiation of the GABA-induced currents by the partial agonist bretazenil. Furthermore, Ro 15-4513, an inverse agonist at wild-type receptors, acts as an agonist at all mutant receptors. This conserved molecular switch can be exploited to identify the pharmacological significance of specific GABA(A)-receptor subtypes in vivo. application/pdf https://sonar.ch/global/documents/185692 eng info:eu-repo/semantics/altIdentifier/doi/10.1016/s0014-5793(98)00803-5 info:eu-repo/semantics/altIdentifier/pmid/9714551 info:eu-repo/semantics/openAccess FEBS letters. - 1998 Amino Acid Sequence Animals Azides Base Sequence Benzodiazepines Benzodiazepinones Cell Line Diazepam Humans Molecular Sequence Data Mutagenesis, Site-Directed Oligodeoxyribonucleotides Patch-Clamp Techniques Rats Receptors, GABA-A Recombinant Proteins Pharmacology of recombinant gamma-aminobutyric acidA receptors rendered diazepam-insensitive by point-mutated alpha-subunits. http://purl.org/coar/resource_type/c_6501