ArticleProceedings of the National Academy of Sciences of the United States of America2011
Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 54 citations in OpenAlex.
- Article
- 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
- 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
- Off-resonanceJournal of biomolecular NMR · 2021Article
- Structural biology of human GPCR drugs and endogenous ligands - insights from NMR spectroscopy.Methods (San Diego, Calif.) · 2020Review
- Quantum Mechanical and Molecular Mechanics Modeling of Membrane-Embedded Rhodopsins.The Journal of membrane biology · 2019Review
- Synthesis of 9-CDTetrahedron letters · 2018Article
- Applications of NMR to membrane proteins.Archives of biochemistry and biophysics · 2017Review
- Solid-State NMR Provides Evidence for Small-Amplitude Slow Domain Motions in a Multispanning Transmembrane α-Helical Protein.Journal of the American Chemical Society · 2017Article
- Powdered G-Protein-Coupled Receptors.The journal of physical chemistry letters · 2016Article
- Quasi-elastic Neutron Scattering Reveals Ligand-Induced Protein Dynamics of a G-Protein-Coupled Receptor.The journal of physical chemistry letters · 2016Article
- CONDENSED-MATTER SPECTROSCOPY SPECTRAL METHODS FOR STUDY OF THE G-PROTEIN-COUPLED RECEPTOR RHODOPSIN. II. MAGNETIC RESONANCE METHODS.Optics and spectroscopy · 2016Article
- Retinal Conformation Changes Rhodopsin's Dynamic Ensemble.Biophysical journal · 2015Article
- Elastic deformation and area per lipid of membranes: atomistic view from solid-state deuterium NMR spectroscopy.Biochimica et biophysica acta · 2015Review
- Investigation of rhodopsin dynamics in its signaling state by solid-state deuterium NMR spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2015Review
- Chemistry and biology of the initial steps in vision: the Friedenwald lecture.Investigative ophthalmology & visual science · 2014Article
- Structural approaches to understanding retinal proteins needed for vision.Current opinion in cell biology · 2014Review
- Retinal ligand mobility explains internal hydration and reconciles active rhodopsin structures.Biochemistry · 2014Article
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Authors and funding
3 authors at 3 institutions in 3 countries.
Funding
Abstract
Rhodopsin is a canonical member of the family of G protein-coupled receptors, which transmit signals across cellular membranes and are linked to many drug interventions in humans. Here we show that solid-state (2)H NMR relaxation allows investigation of light-induced changes in local ps-ns time scale motions of retinal bound to rhodopsin. Site-specific (2)H labels were introduced into methyl groups of the retinal ligand that are essential to the activation process. We conducted solid-state (2)H NMR relaxation (spin-lattice, T(1Z), and quadrupolar-order, T(1Q)) experiments in the dark, Meta I, and Meta II states of the photoreceptor. Surprisingly, we find the retinylidene methyl groups exhibit site-specific differences in dynamics that change upon light excitation--even more striking, the C9-methyl group is a dynamical hotspot that corresponds to a crucial functional hotspot of rhodopsin. Following 11-cis to trans isomerization, the (2)H NMR data suggest the β-ionone ring remains in its hydrophobic binding pocket in all three states of the protein. We propose a multiscale activation mechanism with a complex energy landscape, whereby the photonic energy is directed against the E2 loop by the C13-methyl group, and toward helices H3 and H5 by the C5-methyl of the β-ionone ring. Changes in retinal structure and dynamics initiate activating fluctuations of transmembrane helices H5 and H6 in the Meta I-Meta II equilibrium of rhodopsin. Our proposals challenge the Standard Model whereby a single light-activated receptor conformation yields the visual response--rather an ensemble of substates is present, due to the entropy gain produced by photolysis of the inhibitory retinal lock.
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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.