ArticleInternational journal of molecular sciences2021
Search for Structural Basis of Interactions of Biogenic Amines with Human TAAR1 and TAAR6 Receptors.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers, 1 of them a synthesis that pooled it.
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Who cites it
9 citing papers in PubMed, 1 synthesis or guideline pooled it, 11 citations in OpenAlex.
- Public Transcriptomic Data Meta-Analysis Demonstrates TAAR6 Expression in the Mental Disorder-Related Brain Areas in Human and Mouse Brain.Biomolecules · 2022Pooled it
- Potential of Small Molecule TAAR-1 Agonists for the Therapy of Neurodegenerative Psychosis: A Medicinal Chemistry Perspective.Mini reviews in medicinal chemistry · 2026Review
- JP-14: A Trace Amine-Associated Receptor 1 Agonist with Anti-Metabolic Disorder Potential.International journal of molecular sciences · 2025Article
- Computational Methods for the Discovery and Optimization of TAAR1 and TAAR5 Ligands.International journal of molecular sciences · 2024Review
- Unlocking the secrets of trace amine-associated receptor 1 agonists: new horizon in neuropsychiatric treatment.Frontiers in psychiatry · 2024Review
- Structure-Based Discovery of Mouse Trace Amine-Associated Receptor 5 Antagonists.Journal of chemical information and modeling · 2023Article
- Protein Metabolism Changes and Alterations in Behavior of Trace Amine-Associated Receptor 1 Knockout Mice Fed a High-Fructose Diet.Neurology international · 2023Article
- Article
- Allosteric Modulators of G Protein-Coupled Receptors.International journal of molecular sciences · 2022Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
Abstract
The identification and characterization of ligand-receptor binding sites are important for drug development. Trace amine-associated receptors (TAARs, members of the class A GPCR family) can interact with different biogenic amines and their metabolites, but the structural basis for their recognition by the TAARs is not well understood. In this work, we have revealed for the first time a group of conserved motifs (fingerprints) characterizing TAARs and studied the docking of aromatic (β-phenylethylamine, tyramine) and aliphatic (putrescine and cadaverine) ligands, including gamma-aminobutyric acid, with human TAAR1 and TAAR6 receptors. We have identified orthosteric binding sites for TAAR1 (Asp68, Asp102, Asp284) and TAAR6 (Asp78, Asp112, Asp202). By analyzing the binding results of 7500 structures, we determined that putrescine and cadaverine bind to TAAR1 at one site, Asp68 + Asp102, and to TAAR6 at two sites, Asp78 + Asp112 and Asp112 + Asp202. Tyramine binds to TAAR6 at the same two sites as putrescine and cadaverine and does not bind to TAAR1 at the selected Asp residues. β-Phenylethylamine and gamma-aminobutyric acid do not bind to the TAAR1 and TAAR6 receptors at the selected Asp residues. The search for ligands targeting allosteric and orthosteric sites of TAARs has excellent pharmaceutical potential.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.