ArticleScience (New York, N.Y.)2015
SIGNAL TRANSDUCTION. Structural basis for nucleotide exchange in heterotrimeric G proteins.
Article in Science (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 176 papers.
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Who cites it
176 citing papers in PubMed.
- Innovative Approach Reveals How Receptors Control G Protein State Equilibria.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Atomic, structural and molecular insights into GPCR ligand binding and signalling.Nature reviews. Molecular cell biology · 2026Review
- μ-Opioid ligands tune G-protein opening kinetics.Nature structural & molecular biology · 2026Article
- Ligand-dependent G protein dynamics underlying opioid efficacy.Nature structural & molecular biology · 2026Article
- Structural basis of stepwise G protein activation by the viral chemokine receptor US28.bioRxiv : the preprint server for biology · 2026Article
- Protein Frustration Reveals Orthosteric and Allosteric Active Sites in GPCR:G Protein Complexes.Journal of chemical information and modeling · 2026Article
- Conserved residues in the Gα interface show subtype specificity in Gβγ coupling.The Journal of biological chemistry · 2026Article
- In Vitro Characterization of Agonist and Antagonist Peptide Binding Interaction Kinetics to GLP-1R in HEK293T Cells Using Surface Plasmon Resonance Microscopy.ACS medicinal chemistry letters · 2026Article
- Article
- Allostery between Distant Structural Regions Dictates Selectivity in GPCR:G Protein Coupling.Biochemistry · 2026Article
- Conserved Residues in the Gα interface show subtype specificity in Gβγ coupling.bioRxiv : the preprint server for biology · 2026Article
- Characterization of the GTPγS release function of a G protein-coupled receptor.Nature communications · 2025Article
- Article
- Dissociation kinetics of G proteins from G protein-coupled receptors and effects of allosteric modulation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Non-canonical GScientific reports · 2025Article
- Ligand-dependent G protein dynamics underlying opioid signaling efficacy.bioRxiv : the preprint server for biology · 2025Article
- Christian Bohr. Discoverer of Homotropic and Heterotopic Allostery: Periods Leading up to Bohr's Life, Work, and Beyond. Was Bohr a Vitalist and Right About a "Specific Activity"?Acta physiologica (Oxford, England) · 2025Review
- Hidden GPCR structural transitions addressed by multiple walker supervised molecular dynamics (mwSuMD).eLife · 2025Article
- Virtual library docking for cannabinoid-1 receptor agonists with reduced side effects.Nature communications · 2025Article
- Molecular insights into the modulation of the 5HTFEBS letters · 2025Article
116 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
14 authors.
Funding
Abstract
G protein-coupled receptors (GPCRs) relay diverse extracellular signals into cells by catalyzing nucleotide release from heterotrimeric G proteins, but the mechanism underlying this quintessential molecular signaling event has remained unclear. Here we use atomic-level simulations to elucidate the nucleotide-release mechanism. We find that the G protein α subunit Ras and helical domains-previously observed to separate widely upon receptor binding to expose the nucleotide-binding site-separate spontaneously and frequently even in the absence of a receptor. Domain separation is necessary but not sufficient for rapid nucleotide release. Rather, receptors catalyze nucleotide release by favoring an internal structural rearrangement of the Ras domain that weakens its nucleotide affinity. We use double electron-electron resonance spectroscopy and protein engineering to confirm predictions of our computationally determined mechanism.
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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.