ArticleInvertebrate neuroscience : IN2007
The channel-lining 6' amino acid in the second membrane-spanning region of ionotropic GABA receptors has more profound effects on 4'-ethynyl-4-n-propylbicycloorthobenzoate binding than the 2' amino acid.
Article in Invertebrate neuroscience : IN, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 30 citations in OpenAlex.
- Identification of The Fipronil Resistance Associated Mutations inMolecules (Basel, Switzerland) · 2019Article
- The dual modulatory effects of efavirenz on GABANeuropharmacology · 2017Article
- Methylene blue inhibits GABANeuropharmacology · 2017Article
- GABAA receptor target of tetramethylenedisulfotetramine.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Probing structural features and binding mode of 3-arylpyrimidin-2,4-diones within housefly γ-aminobutyric acid (GABA) receptor.International journal of molecular sciences · 2011Article
- Homology modeling of human alpha 1 beta 2 gamma 2 and house fly beta 3 GABA receptor channels and Surflex-docking of fipronil.Journal of molecular modeling · 2009Article
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
The noncompetitive antagonist of ionotropic gamma-aminobutyric acid (GABA) receptors 4'-ethynyl-4-n-propylbicycloorthobenzoate (EBOB) is a useful tool to probe the antagonist-binding site. In the present study, four mutants of the human GABA(A) receptor beta3 subunit were stably expressed in S2 cells and examined for their abilities to bind [(3)H]EBOB to identify the binding site of EBOB. The homo-oligomeric beta3 GABA receptor was used as a housefly GABA receptor model, as the beta3 subunit has a high sequence similarity with the housefly Rdl subunit in the second membrane-spanning (M2) region. The A274S mutation at the -1' position in the M2 region had no effect on [(3)H]EBOB binding. The A277S mutation at the 2' position led to a decrease in the affinity of EBOB for the GABA receptor. The T281V mutant at the 6' position and the A277S/T281V double mutant completely abolished the binding ability. A beta3 GABA receptor homology model predicts these interactions between the receptor and EBOB. These results suggest that EBOB interacts with threonine 281 and alanine 277, and that threonine 281 plays a more critical role in interacting with EBOB than alanine 277.
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