ArticleNature communications2016
Retinal orientation and interactions in rhodopsin reveal a two-stage trigger mechanism for activation.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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Who cites it
25 citing papers in PubMed.
- Conformational signatures of native ligand and pharmacochaperone binding in rhodopsin.Structure (London, England : 1993) · 2026Article
- Therapeutic Potential of Partial Retinoid Agonists against Vertebrate Rhodopsin Misfolding Disorders.ACS omega · 2025Article
- In-silico predicted mouse melanopsins with blue spectral shifts deliver efficient subcellular signaling.Cell communication and signaling : CCS · 2024Article
- Solid-state NMR of the retinal protonated Schiff base in microbial rhodopsins.Magnetic resonance letters · 2024Review
- Coordination of bilayer properties by an inward-rectifier KJournal of structural biology: X · 2024Article
- Strategies for acquisition of resonance assignment spectra of highly dynamic membrane proteins: a GPCR case study.Journal of biomolecular NMR · 2023Article
- Cholesterol Biases the Conformational Landscape of the Chemokine Receptor CCR3: A MAS SSNMR-Filtered Molecular Dynamics Study.Journal of chemical information and modeling · 2023Article
- Article
- Rhodopsin-associated retinal dystrophy: Disease mechanisms and therapeutic strategies.Frontiers in neuroscience · 2023Review
- Hydration-mediated G-protein-coupled receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Magic angle spinning NMR of G protein-coupled receptors.Progress in nuclear magnetic resonance spectroscopy · 2022Review
- Deconstructing the transmembrane core of class A G protein-coupled receptors.Trends in biochemical sciences · 2021Review
- Probing the photointermediates of light-driven sodium ion pump KR2 by DNP-enhanced solid-state NMR.Science advances · 2021Article
- Structure of a retinal chromophore of dark-adapted middle rhodopsin as studied by solid-state nuclear magnetic resonance spectroscopy.Biophysics and physicobiology · 2021Article
- A Conserved Proline Hinge Mediates Helix Dynamics and Activation of Rhodopsin.Structure (London, England : 1993) · 2020Article
- Structural biology of human GPCR drugs and endogenous ligands - insights from NMR spectroscopy.Methods (San Diego, Calif.) · 2020Review
- Conformational perturbation, allosteric modulation of cellular signaling pathways, and disease in P23H rhodopsin.Scientific reports · 2020Article
- The Retinoid and Non-Retinoid Ligands of the Rod Visual G Protein-Coupled Receptor.International journal of molecular sciences · 2019Review
- Crystal structure of jumping spider rhodopsin-1 as a light sensitive GPCR.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Crystal structure of rhodopsin in complex with a mini-GScience advances · 2018Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
The 11-cis retinal chromophore is tightly packed within the interior of the visual receptor rhodopsin and isomerizes to the all-trans configuration following absorption of light. The mechanism by which this isomerization event drives the outward rotation of transmembrane helix H6, a hallmark of activated G protein-coupled receptors, is not well established. To address this question, we use solid-state NMR and FTIR spectroscopy to define the orientation and interactions of the retinal chromophore in the active metarhodopsin II intermediate. Here we show that isomerization of the 11-cis retinal chromophore generates strong steric interactions between its β-ionone ring and transmembrane helices H5 and H6, while deprotonation of its protonated Schiff's base triggers the rearrangement of the hydrogen-bonding network involving residues on H6 and within the second extracellular loop. We integrate these observations with previous structural and functional studies to propose a two-stage mechanism for rhodopsin activation.
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