ArticleAngewandte Chemie (International ed. in English)2020
Light Dynamics of the Retinal-Disease-Relevant G90D Bovine Rhodopsin Mutant.
Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Human cells for human proteins: Isotope labeling in mammalian cells in suspension for functional NMR studies.Protein science : a publication of the Protein Society · 2026Article
- Dynamic nuclear polarization and chemically induced hyperpolarization: Progress, mechanisms, and opportunities.Magnetic resonance letters · 2025Review
- Dark continuous noise from mutant G90D-rhodopsin predominantly underlies congenital stationary night blindness.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Molecular mechanisms and evolutionary robustness of a color switch in proteorhodopsins.Science advances · 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
- Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics.Magnetic resonance (Gottingen, Germany) · 2021Review
- Light Dynamics of the Retinal-Disease-Relevant G90D Bovine Rhodopsin Mutant.Angewandte Chemie (International ed. in English) · 2020Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The RHO gene encodes the G-protein-coupled receptor (GPCR) rhodopsin. Numerous mutations associated with impaired visual cycle have been reported; the G90D mutation leads to a constitutively active mutant form of rhodopsin that causes CSNB disease. We report on the structural investigation of the retinal configuration and conformation in the binding pocket in the dark and light-activated state by solution and MAS-NMR spectroscopy. We found two long-lived dark states for the G90D mutant with the 11-cis retinal bound as Schiff base in both populations. The second minor population in the dark state is attributed to a slight shift in conformation of the covalently bound 11-cis retinal caused by the mutation-induced distortion on the salt bridge formation in the binding pocket. Time-resolved UV/Vis spectroscopy was used to monitor the functional dynamics of the G90D mutant rhodopsin for all relevant time scales of the photocycle. The G90D mutant retains its conformational heterogeneity during the photocycle.
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