ArticleBritish journal of pharmacology2015
Identification of the putative binding pocket of valerenic acid on GABAA receptors using docking studies and site-directed mutagenesis.
Article in British journal of pharmacology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Decoding the structural and functional diversity of GABAFrontiers in pharmacology · 2025Review
- Structural insights into GABANature communications · 2024Article
- Site-Directed Mutation of Salicylate Decarboxylase Gene and Mechanism of Ginkgo Acid Decarboxylation.The protein journal · 2023Article
- Docking-Based Prediction of Peptide Binding to MHC Proteins.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Novel Potent and Selective Agonists of the GPR55 Receptor Based on the 3-Benzylquinolin-2(1Pharmaceuticals (Basel, Switzerland) · 2022Article
- Recent Advances in In Silico Target Fishing.Molecules (Basel, Switzerland) · 2021Review
- Biological Profiling of Semisynthetic C19-Functionalized Ferruginol and Sugiol Analogues.Antibiotics (Basel, Switzerland) · 2021Article
- "Effect of valerenic acid on neuroinflammation in a MPTP-induced mouse model of Parkinson's disease".IBRO reports · 2020Article
- Article
- Discovery of Novel µ-Opioid Receptor Inverse Agonist from a Combinatorial Library of Tetrapeptides through Structure-Based Virtual Screening.Molecules (Basel, Switzerland) · 2019Article
- Metabolic Products of Linalool and Modulation of GABAFrontiers in chemistry · 2017Article
- Analysis of β-Subunit-dependent GABAA Receptor Modulation and Behavioral Effects of Valerenic Acid Derivatives.The Journal of pharmacology and experimental therapeutics · 2016Article
- Novel positive allosteric modulators of GABAA receptors with anesthetic activity.Scientific reports · 2016Article
- Structural Studies of GABAA Receptor Binding Sites: Which Experimental Structure Tells us What?Frontiers in molecular neuroscience · 2016Article
- Identification of the putative binding pocket of valerenic acid on GABAA receptors using docking studies and site-directed mutagenesis.British journal of pharmacology · 2015Article
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12 authors.
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Abstract
background and purposeβ2/3-subunit-selective modulation of GABAA receptors by valerenic acid (VA) is determined by the presence of transmembrane residue β2/3N265. Currently, it is not known whether β2/3N265 is part of VA's binding pocket or is involved in the transduction pathway of VA's action. The aim of this study was to clarify the localization of VA's binding pocket on GABAA receptors. EXPERIMENTAL APPROACH: Docking and a structure-based three-dimensional pharmacophore were employed to identify candidate amino acid residues that are likely to interact with VA. Selected amino acid residues were mutated, and VA-induced modulation of the resulting GABAA receptors expressed in Xenopus oocytes was analysed. KEY
resultsA binding pocket for VA at the β(+) /α(-) interface encompassing amino acid β3N265 was predicted. Mutational analysis of suggested amino acid residues revealed a complete loss of VA's activity on β3M286W channels as well as significantly decreased efficacy and potency of VA on β3N265S and β3F289S receptors. In addition, reduced efficacy of VA-induced IGABA enhancement was also observed for α1M235W, β3R269A and β3M286A constructs. CONCLUSIONS AND IMPLICATIONS: Our data suggest that amino acid residues β3N265, β3F289, β3M286, β3R269 in the β3 subunit, at or near the etomidate/propofol binding site(s), form part of a VA binding pocket. The identification of the binding pocket for VA is essential for elucidating its pharmacological effects and might also help to develop new selective GABAA receptor ligands.
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