ArticleThe Journal of biological chemistry2012
Role of detergents in conformational exchange of a G protein-coupled receptor.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- Stabilization versus flexibility: Detergent-dependent trade-offs in neurotensin receptor 1 GPCR ensembles.Protein science : a publication of the Protein Society · 2026Article
- The influence of lipids and biological membranes on the conformational equilibria of GPCRs: Insights from NMR spectroscopy.Current opinion in structural biology · 2025Review
- Stabilization versus flexibility: detergent-dependent trade-offs in neurotensin receptor 1 GPCR ensembles.bioRxiv : the preprint server for biology · 2025Article
- Direct effect of membrane environment on the activation of mGluR2 revealed by single-molecule FRET.Structure (London, England : 1993) · 2025Article
- Monitoring conformational changes in the human neurotransmitter transporter homologue LeuT withJournal of neurochemistry · 2025Article
- Membrane mimetic-dependence of GPCR energy landscapes.Structure (London, England : 1993) · 2024Article
- Anomalous Oligomerization Behavior ofInternational journal of molecular sciences · 2023Article
- Sub-millisecond conformational dynamics of the ACommunications biology · 2023Article
- Rapid and Highly Stable Membrane Reconstitution by LAiR Enables the Study of Physiological Integral Membrane Protein Functions.ACS central science · 2023Article
- GPCR structural characterization by NMR spectroscopy in solution.Acta biochimica et biophysica Sinica · 2022Review
- G Protein-coupled Receptor (GPCR) Reconstitution and Labeling for Solution Nuclear Magnetic Resonance (NMR) Studies of the Structural Basis of Transmembrane Signaling.Molecules (Basel, Switzerland) · 2022Review
- Function-Related Dynamics in Multi-Spanning Helical Membrane Proteins Revealed by Solution NMR.Membranes · 2021Review
- DEER Analysis of GPCR Conformational Heterogeneity.Biomolecules · 2021Review
- Mass Photometry of Membrane Proteins.Chem · 2021Article
- The Conformational Equilibrium of the Neuropeptide Y2 Receptor in Bilayer Membranes.Angewandte Chemie (International ed. in English) · 2020Article
- Activation Microswitches in Adenosine Receptor ABiochemistry · 2020Article
- Structure and Dynamics of GPCRs in Lipid Membranes: Physical Principles and Experimental Approaches.Molecules (Basel, Switzerland) · 2020Review
- Capturing Peptide-GPCR Interactions and Their Dynamics.Molecules (Basel, Switzerland) · 2020Review
- Unveiling the activation dynamics of a fold-switch bacterial glycosyltransferase byThe Journal of biological chemistry · 2020Article
- How Do Branched Detergents Stabilize GPCRs in Micelles?Biochemistry · 2020Article
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6 authors.
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Abstract
The G protein-coupled β(2)-adrenoreceptor (β(2)AR) signals through the heterotrimeric G proteins G(s) and G(i) and β-arrestin. As such, the energy landscape of β(2)AR-excited state conformers is expected to be complex. Upon tagging Cys-265 of β(2)AR with a trifluoromethyl probe, (19)F NMR was used to assess conformations and possible equilibria between states. Here, we report key differences in β(2)AR conformational dynamics associated with the detergents used to stabilize the receptor. In dodecyl maltoside (DDM) micelles, the spectra are well represented by a single Lorentzian line that shifts progressively downfield with activation by appropriate ligand. The results are consistent with interconversion between two or more states on a time scale faster than the greatest difference in ligand-dependent chemical shift (i.e. >100 Hz). Given that high detergent off-rates of DDM monomers may facilitate conformational exchange between functional states of β(2)AR, we utilized the recently developed maltose-neopentyl glycol (MNG-3) diacyl detergent. In MNG-3 micelles, spectra indicated at least three distinct states, the relative populations of which depended on ligand, whereas no ligand-dependent shifts were observed, consistent with the slow exchange limit. Thus, detergent has a profound effect on the equilibrium kinetics between functional states. MNG-3, which has a critical micelle concentration in the nanomolar regime, exhibits an off-rate that is 4 orders of magnitude lower than that of DDM. High detergent off-rates are more likely to facilitate conformational exchange between distinct functional states associated with the G protein-coupled receptor.
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