The DOI matches its Crossref record; 76 of the 76 references it cites were found in a registry or an index.
Structure of a human synaptic GABAA receptor
Open accessAbstract
Fast inhibitory neurotransmission in the brain is principally mediated by the neurotransmitter GABA (γ-aminobutyric acid) and its synaptic target, the type A GABA receptor (GABAA receptor). Dysfunction of this receptor results in neurological disorders and mental illnesses including epilepsy, anxiety and insomnia. The GABAA receptor is also a prolific target for therapeutic, illicit and recreational drugs, including benzodiazepines, barbiturates, anaesthetics and ethanol. Here we present high-resolution cryo-electron microscopy structures of the human α1β2γ2 GABAA receptor, the predominant isoform in the adult brain, in complex with GABA and the benzodiazepine site antagonist flumazenil, the first-line clinical treatment for benzodiazepine overdose. The receptor architecture reveals unique heteromeric interactions for this important class of inhibitory neurotransmitter receptor. This work provides a template for understanding receptor modulation by GABA and benzodiazepines, and will assist rational approaches to therapeutic targeting of this receptor for neurological disorders and mental illness. The cryo-electron microscopy structure of the type A GABA receptor bound to GABA and the benzodiazepine site antagonist flumazenil reveals structural mechanisms that underlie intersubunit interactions and ligand selectivity of the receptor.
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Metadata
- Authors
- Zhu, S., Noviello, C. M., Teng, J., Walsh, R. M., Kim, J. J., & Hibbs, R. E.
- Venue
- Nature
- Published
- 2018-06-27
- Volume
- 559
- Issue
- 7712
- Pages
- 67-72
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2810911197
- Cited by
- 549
- References
- 76
- FWCI
- 21.68
- Type
- journal article
- Language
- en
- Open access
- green
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