ArticleProceedings of the National Academy of Sciences of the United States of America2019
Diverse GPCRs exhibit conserved water networks for stabilization and activation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers, 1 of them a synthesis that pooled it.
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Who cites it
86 citing papers in PubMed, 1 synthesis or guideline pooled it.
- GWAS of random glucose in 476,326 individuals provide insights into diabetes pathophysiology, complications and treatment stratification.Nature genetics · 2023Pooled it
- Atomic, structural and molecular insights into GPCR ligand binding and signalling.Nature reviews. Molecular cell biology · 2026Review
- Biophysical and structural analysis of human green cone opsin.Biophysical journal · 2026Article
- Structured water molecules drive activation and G protein selectivity in the GPR174 receptor.PLoS biology · 2026Article
- Structural mechanisms underlying distinct binding and activities of 18:0 and 18:1 lysophosphatidic acids at LPA1 receptor.PLoS computational biology · 2026Article
- Direct evidence of acid-driven protein desolvation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Structural analysis reveals that water molecules mediate self-activation of GPR99.Communications biology · 2026Article
- Identifying Functional Water Encapsulation Sites Within the Transmembrane Domain of Sensor Kinases.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Integration of GPCR Modeling with QM for Drug Design: Academic and Industry Collaboration.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Human Serum Albumin: 3D Insight on Protein Hydration.International journal of molecular sciences · 2025Article
- Superwater as a generative AI framework to predict water molecule positions on protein structures.Communications chemistry · 2025Article
- Structure of human green cone opsin yields insights into mechanisms underlying the rapid decay of its active, signaling state.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Effect of a Low Electrostatic Environment on the Helical Structures of Peptides and Proteins Using Flexible Water Models: An In Silico Study.ACS omega · 2025Article
- An active allosteric mechanism in ASAP1-mediated Arf1 GTP hydrolysis redefines PH domain function.Nature communications · 2025Article
- Enhanced Sampling and Tailored Collective Variables Yield Reproducible Free Energy Landscapes of Beta-1 Adrenergic Receptor Activation.Journal of chemical theory and computation · 2025Article
- Docking 14 Million Virtual Isoquinuclidines against the μ and κ Opioid Receptors Reveals Dual Antagonists-Inverse Agonists with Reduced Withdrawal Effects.ACS central science · 2025Article
- EnGCI: enhancing GPCR-compound interaction prediction via large molecular models and KAN network.BMC biology · 2025Article
- Discovering Key Activation Hotspots in the MJournal of the American Chemical Society · 2025Article
- Structural insights into lipid chain-length selectivity and allosteric regulation of FFA2.Nature communications · 2025Article
- Computational design of highly signalling-active membrane receptors through solvent-mediated allosteric networks.Nature chemistry · 2025Article
26 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors.
Funding
Abstract
G protein-coupled receptors (GPCRs) have evolved to recognize incredibly diverse extracellular ligands while sharing a common architecture and structurally conserved intracellular signaling partners. It remains unclear how binding of diverse ligands brings about GPCR activation, the common structural change that enables intracellular signaling. Here, we identify highly conserved networks of water-mediated interactions that play a central role in activation. Using atomic-level simulations of diverse GPCRs, we show that most of the water molecules in GPCR crystal structures are highly mobile. Several water molecules near the G protein-coupling interface, however, are stable. These water molecules form two kinds of polar networks that are conserved across diverse GPCRs: (
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