ArticleProceedings of the National Academy of Sciences of the United States of America2012
Effect of channel mutations on the uptake and release of the retinal ligand in opsin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 81 citations in OpenAlex.
- New Fluorescent Probes for Visual Proteins. Part III. Probing Auxiliary Gateways and the Stepwise Activation Model of Ligand Transport.Journal of fluorescence · 2026Article
- The microbiome of marine mat-forming cyanobacteria-a microcosm of taxonomic novelty and phototrophic diversity.ISME communications · 2026Article
- A key amino acid site associated with rhodopsin mammal evolution to diurnal vision.Scientific reports · 2025Article
- Bioluminescence and environmental light drive the visual evolution of deep-sea shrimp (Oplophoroidea).Communications biology · 2025Article
- Structural insights into the mechanism and dynamics of proteorhodopsin biogenesis and retinal scavenging.Nature communications · 2024Article
- Chromenone derivatives as novel pharmacological chaperones for retinitis pigmentosa-linked rod opsin mutants.Human molecular genetics · 2022Article
- FRET sensors reveal the retinal entry pathway in the G protein-coupled receptor rhodopsin.iScience · 2022Article
- Two entry tunnels in mouse TAAR9 suggest the possibility of multi-entry tunnels in olfactory receptors.Scientific reports · 2022Article
- New insights into the molecular mechanism of rhodopsin retinitis pigmentosa from the biochemical and functional characterization of G90V, Y102H and I307N mutations.Cellular and molecular life sciences : CMLS · 2022Article
- Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.Frontiers in chemistry · 2022Review
- Evolutionary adaptation of visual pigments in geckos for their photic environment.Science advances · 2021Article
- Opsins outside the eye and the skin: a more complex scenario than originally thought for a classical light sensor.Cell and tissue research · 2021Review
- Recurrent convergent evolution at amino acid residue 261 in fish rhodopsin.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- To see or not to see: molecular evolution of the rhodopsin visual pigment in neotropical electric fishes.Proceedings. Biological sciences · 2019Article
- Article
- Entry from the Lipid Bilayer: A Possible Pathway for Inhibition of a Peptide G Protein-Coupled Receptor by a Lipophilic Small Molecule.Biochemistry · 2018Article
- Full rescue of an inactive olfactory receptor mutant by elimination of an allosteric ligand-gating site.Scientific reports · 2018Article
- Ligand channel in pharmacologically stabilized rhodopsin.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Human Blue Cone Opsin Regeneration Involves Secondary Retinal Binding with Analog Specificity.Biophysical journal · 2018Article
- Dynamical Binding Modes Determine Agonistic and Antagonistic Ligand Effects in the Prostate-Specific G-Protein Coupled Receptor (PSGR).Scientific reports · 2017Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the retinal binding pocket of rhodopsin, a Schiff base links the retinal ligand covalently to the Lys296 side chain. Light transforms the inverse agonist 11-cis-retinal into the agonist all-trans-retinal, leading to the active Meta II state. Crystal structures of Meta II and the active conformation of the opsin apoprotein revealed two openings of the 7-transmembrane (TM) bundle towards the hydrophobic core of the membrane, one between TM1/TM7 and one between TM5/TM6, respectively. Computational analysis revealed a putative ligand channel connecting the openings and traversing the binding pocket. Identified constrictions within the channel motivated this study of 35 rhodopsin mutants in which single amino acids lining the channel were replaced. 11-cis-retinal uptake and all-trans-retinal release were measured using UV/visible and fluorescence spectroscopy. Most mutations slow or accelerate both uptake and release, often with opposite effects. Mutations closer to the Lys296 active site show larger effects. The nucleophile hydroxylamine accelerates retinal release 80 times but the action profile of the mutants remains very similar. The data show that the mutations do not probe local channel permeability but rather affect global protein dynamics, with the focal point in the ligand pocket. We propose a model for retinal/receptor interaction in which the active receptor conformation sets the open state of the channel for 11-cis-retinal and all-trans-retinal, with positioning of the ligand at the active site as the kinetic bottleneck. Although other G protein-coupled receptors lack the covalent link to the protein, the access of ligands to their binding pocket may follow similar schemes.
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