ArticleNature communications2023
Thermodynamic architecture and conformational plasticity of GPCRs.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 30 citations in OpenAlex.
- A Transferable and Robust Computational Framework for Class A GPCR Activation Free Energies.The journal of physical chemistry letters · 2026Article
- Selective control of ligand binding through a distal mutation that alters the protein native ensemble.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Do GPCRs constitute the target of 30% of newly approved drugs in Germany?Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- Fine-Tuning of the Neuropeptide Y1 G Protein-Coupled Receptor by the TryptophanJournal of the American Chemical Society · 2026Article
- Structural Basis of GPCR-Biased Modulation.Handbook of experimental pharmacology · 2026Review
- An update for AlphaFold3 versus experimental structures: assessing the precision of small molecule binding in GPCRs.Acta pharmacologica Sinica · 2025Article
- Local and Global Breathing Motions Prime the Access to Buried Binding Site in an Antibiotic-Sequestering Protein.ACS bio & med chem Au · 2025Article
- Unlocking therapeutic potential in traumatic brain injury: exploring microenvironmental targets, signaling pathways and translational hurdles.Inflammopharmacology · 2025Review
- Exploring Conformational Transitions in Biased and Balanced Ligand Binding of GLP-1R.Molecules (Basel, Switzerland) · 2025Article
- Temporal complexity of LVV-hemorphin-7 allosterism at the angiotensin II type 1 receptor assessed using entropy-based approaches.Computational and structural biotechnology journal · 2025Article
- Investigation of GPR137C as a promising novel marker for the progression of prostate cancer through G4 screen and bioinformatics analyses.Frontiers in immunology · 2025Article
- Molecular Determinant Underlying Selective Coupling of Primary G-Protein by Class A GPCRs.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- A finely balanced order-disorder equilibrium sculpts the folding-binding landscape of an antibiotic sequestering protein.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Molecular and thermodynamic determinants of self-assembly and hetero-oligomerization in the enterobacterial thermo-osmo-regulatory protein H-NS.Nucleic acids research · 2024Article
- Evaluating conserved domains and motifs of decapod gonadotropin-releasing hormone G protein-coupled receptor superfamily.Frontiers in endocrinology · 2024Article
- Conformational Tuning Shapes the Balance between Functional Promiscuity and Specialization in ParalogousBiochemistry · 2023Article
- AIMD-Chig: Exploring the conformational space of a 166-atom protein Chignolin with ab initio molecular dynamics.Scientific data · 2023Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
G-protein-coupled receptors (GPCRs) are ubiquitous integral membrane proteins involved in diverse cellular signaling processes. Here, we carry out a large-scale ensemble thermodynamic study of 45 ligand-free GPCRs employing a structure-based statistical mechanical framework. We find that multiple partially structured states co-exist in the GPCR native ensemble, with the TM helices 1, 6 and 7 displaying varied folding status, and shaping the conformational landscape. Strongly coupled residues are anisotropically distributed, accounting for only 13% of the residues, illustrating that a large number of residues are inherently dynamic. Active-state GPCRs are characterized by reduced conformational heterogeneity with altered coupling-patterns distributed throughout the structural scaffold. In silico alanine-scanning mutagenesis reveals that extra- and intra-cellular faces of GPCRs are coupled thermodynamically, highlighting an exquisite structural specialization and the fluid nature of the intramolecular interaction network. The ensemble-based perturbation methodology presented here lays the foundation for understanding allosteric mechanisms and the effects of disease-causing mutations in GCPRs.
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Registered trials
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.