期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1991
卷号：88
期号：4
页码：1421-1425
DOI：10.1073/pnas.88.4.1421
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Recombinantly expressed gamma-aminobutyric acid type A (GABAA) receptors consisting of alpha 1, beta 2, and gamma 2 subunits contain a binding site for benzodiazepines that differs in its properties from that of alpha 3 beta 2 gamma 2 receptors. Amino acid substitutions between the GABAA receptor alpha subunits were analyzed for their effect on the binding of compounds to the benzodiazepine site. By converting ever smaller regions of the alpha 3 subunit sequence to that of the alpha 1 subunit, we show that a single substitution (glycine for glutamic acid) increases the affinity for several compounds approximately 10-fold without changing the affinity for nonselective compounds. Hence, the identified amino acids may interact directly with the ligand and define part of the benzodiazepine binding sites in these receptors.
