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- W2038477005 abstract "The GABAA receptor belongs, along with the nicotinic acetylcholine receptor, the glycine receptor and the 5-HT3 receptor, to a family of homologous transmitter-gated ion channels mediating fast synaptic transmission. Many classes of drug interact with the GABAA receptor, which is the major inhibitory ion channel in the mammalian brain. Among these drugs are the allosteric modulators acting at the benzodiazepine binding site. In this article, Erwin Sigel and Andreas Buhr discuss recent studies that have identified amino acid residues that are thought to form the binding pocket for these compounds. These residues are probably located at subunit interfaces of the protein pentamer and at least some of them are homologous to residues implicated in channel agonist binding. This implies pseudosymmetry of channel agonist and channel modulatory sites, which may be, as recent data indicate, a general principle realized in other pseudosymmetric protein complexes." @default.
- W2038477005 created "2016-06-24" @default.
- W2038477005 creator A5000466780 @default.
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- W2038477005 date "1997-11-01" @default.
- W2038477005 modified "2023-10-11" @default.
- W2038477005 title "The benzodiazepine binding site of GABAA receptors" @default.
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- W2038477005 doi "https://doi.org/10.1016/s0165-6147(97)01118-8" @default.
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