ArticleCellular and molecular life sciences : CMLS2016
Beyond spectral tuning: human cone visual pigments adopt different transient conformations for chromophore regeneration.
Article in Cellular and molecular life sciences : CMLS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Biophysical and structural analysis of human green cone opsin.Biophysical journal · 2026Article
- G-protein activation of the dark-state conformation of the visual G protein-coupled receptor rhodopsin by releasing critical structural constraints.Communications biology · 2026Article
- Engineered red Opto-mGluR6 Opsins, a red-shifted optogenetic excitation tool, an in vitro study.PloS one · 2024Article
- Effect of Trace Metal Ions on the Conformational Stability of the Visual Photoreceptor Rhodopsin.International journal of molecular sciences · 2023Article
- What Makes GPCRs from Different Families Bind to the Same Ligand?Biomolecules · 2022Article
- Human Blue Cone Opsin Regeneration Involves Secondary Retinal Binding with Analog Specificity.Biophysical journal · 2018Article
- Complex binding pathways determine the regeneration of mammalian green cone opsin with a locked retinal analogue.The Journal of biological chemistry · 2017Article
- A G Protein-Coupled Receptor Dimerization Interface in Human Cone Opsins.Biochemistry · 2017Article
- Functional role of positively selected amino acid substitutions in mammalian rhodopsin evolution.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human red and green visual pigments are seven transmembrane receptors of cone photoreceptor cells of the retina that mediate color vision. These pigments share a very high degree of homology and have been assumed to feature analogous structural and functional properties. We report on a different regeneration mechanism among red and green cone opsins with retinal analogs using UV-Vis/fluorescence spectroscopic analyses, molecular modeling and site-directed mutagenesis. We find that photoactivated green cone opsin adopts a transient conformation which regenerates via an unprotonated Schiff base linkage with its natural chromophore, whereas red cone opsin forms a typical protonated Schiff base. The chromophore regeneration kinetics is consistent with a secondary retinal uptake by the cone pigments. Overall, our findings reveal, for the first time, structural differences in the photoactivated conformation between red and green cone pigments that may be linked to their molecular evolution, and support the proposal of secondary retinal binding to visual pigments, in addition to binding to the canonical primary site, which may serve as a regulatory mechanism of dark adaptation in the phototransduction process.
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Registered trials
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.