ArticleJournal of chemical information and modeling2022
Conservation of Allosteric Ligand Binding Sites in G-Protein Coupled Receptors.
Article in Journal of chemical information and modeling, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
14 citing papers in PubMed.
- Effects of Membrane Cholesterol on the Structure and Function of Selected Class A GPCRs─Challenges and Future Perspectives.Biochemistry · 2025Review
- Decoding allosteric landscapes: computational methodologies for enzyme modulation and drug discovery.RSC chemical biology · 2025Review
- Adenosine receptor subtype modulators: Insight into molecular mechanisms and their therapeutic application.American journal of translational research · 2025Review
- Exploring G Protein-Coupled Receptors in Hematological Cancers.ACS pharmacology & translational science · 2024Article
- Comparative Study of Allosteric GPCR Binding Sites and Their Ligandability Potential.Journal of chemical information and modeling · 2024Article
- Structural perspectives on chemokine receptors.Biochemical Society transactions · 2024Review
- G protein-coupled receptors (GPCRs): advances in structures, mechanisms, and drug discovery.Signal transduction and targeted therapy · 2024Review
- Expanding FTMap for Fragment-Based Identification of Pharmacophore Regions in Ligand Binding Sites.Journal of chemical information and modeling · 2024Article
- Article
- An inverse agonist of orphan receptor GPR61 acts by a G protein-competitive allosteric mechanism.Nature communications · 2023Article
- Advances in the allostery of angiotensin II type 1 receptor.Cell & bioscience · 2023Review
- Deep Learning Dynamic Allostery of G-Protein-Coupled Receptors.Research square · 2023Article
- Deep Learning Dynamic Allostery of G-Protein-Coupled Receptors.bioRxiv : the preprint server for biology · 2023Article
- Allosteric crosstalk in modular proteins: Function fine-tuning and drug design.Computational and structural biotechnology journal · 2023Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Despite the growing number of G protein-coupled receptor (GPCR) structures, only 39 structures have been cocrystallized with allosteric inhibitors. These structures have been studied by protein mapping using the FTMap server, which determines the clustering of small organic probe molecules distributed on the protein surface. The method has found druggable sites overlapping with the cocrystallized allosteric ligands in 21 GPCR structures. Mapping of Alphafold2 generated models of these proteins confirms that the same sites can be identified without the presence of bound ligands. We then mapped the 394 GPCR X-ray structures available at the time of the analysis (September 2020). Results show that for each of the 21 structures with bound ligands there exist many other GPCRs that have a strong binding hot spot at the same location, suggesting potential allosteric sites in a large variety of GPCRs. These sites cluster at nine distinct locations, and each can be found in many different proteins. However, ligands binding at the same location generally show little or no similarity, and the amino acid residues interacting with these ligands also differ. Results confirm the possibility of specifically targeting these sites across GPCRs for allosteric modulation and help to identify the most likely binding sites among the limited number of potential locations. The FTMap server is available free of charge for academic and governmental use at https://ftmap.bu.edu/.
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Registered trials
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