ArticleThe Journal of biological chemistry2009
Location of the retinal chromophore in the activated state of rhodopsin*.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 91 citations in OpenAlex.
- Interdisciplinary biophysical studies of membrane proteins bacteriorhodopsin and rhodopsin.Biophysical reviews · 2023Review
- Magic angle spinning NMR of G protein-coupled receptors.Progress in nuclear magnetic resonance spectroscopy · 2022Review
- A Mechanistic Review of β-Carotene, Lutein, and Zeaxanthin in Eye Health and Disease.Antioxidants (Basel, Switzerland) · 2020Review
- Orthologous Divergence and Paralogous Anticonvergence in Molecular Evolution of Triplicated Green Opsin Genes in Medaka Fish, Genus Oryzias.Genome biology and evolution · 2020Article
- Quantum Mechanical and Molecular Mechanics Modeling of Membrane-Embedded Rhodopsins.The Journal of membrane biology · 2019Review
- Photoreaction pathways and photointermediates of retinal-binding photoreceptor proteins as revealed by in situ photoirradiation solid-state NMR spectroscopy.Biophysical reviews · 2019Review
- Article
- Lipids Alter Rhodopsin Function via Ligand-like and Solvent-like Interactions.Biophysical journal · 2018Article
- Article
- Photocyclic behavior of rhodopsin induced by an atypical isomerization mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Chlorophyll-Derivative Modulation of Rhodopsin Signaling Properties through Evolutionarily Conserved Interaction Pathways.Frontiers in molecular biosciences · 2017Article
- Retinal orientation and interactions in rhodopsin reveal a two-stage trigger mechanism for activation.Nature communications · 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
- Retinal Flip in Rhodopsin Activation?Biophysical journal · 2015Article
- Retinal Flips the Script.Biophysical journal · 2015Article
- Model structures of inactive and peptide agonist bound C5aR: Insights into agonist binding, selectivity and activation.Biochemistry and biophysics reports · 2015Article
- Uncovering the triggers for GPCR activation using solid-state NMR spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- 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
11 authors at 4 institutions in 3 countries.
Funding
Abstract
Rhodopsin is a highly specialized G protein-coupled receptor (GPCR) that is activated by the rapid photochemical isomerization of its covalently bound 11-cis-retinal chromophore. Using two-dimensional solid-state NMR spectroscopy, we defined the position of the retinal in the active metarhodopsin II intermediate. Distance constraints were obtained between amino acids in the retinal binding site and specific (13)C-labeled sites located on the beta-ionone ring, polyene chain, and Schiff base end of the retinal. We show that the retinal C20 methyl group rotates toward the second extracellular loop (EL2), which forms a cap on the retinal binding site in the inactive receptor. Despite the trajectory of the methyl group, we observed an increase in the C20-Gly(188) (EL2) distance consistent with an increase in separation between the retinal and EL2 upon activation. NMR distance constraints showed that the beta-ionone ring moves to a position between Met(207) and Phe(208) on transmembrane helix H5. Movement of the ring toward H5 was also reflected in increased separation between the Cepsilon carbons of Lys(296) (H7) and Met(44) (H1) and between Gly(121) (H3) and the retinal C18 methyl group. Helix-helix interactions involving the H3-H5 and H4-H5 interfaces were also found to change in the formation of metarhodopsin II reflecting increased retinal-protein interactions in the region of Glu(122) (H3) and His(211) (H5). We discuss the location of the retinal in metarhodopsin II and its interaction with sequence motifs, which are highly conserved across the pharmaceutically important class A GPCR family, with respect to the mechanism of receptor activation.
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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.