ArticleBiophysical journal2018
Human Blue Cone Opsin Regeneration Involves Secondary Retinal Binding with Analog Specificity.
Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 8 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
- Structure of human green cone opsin yields insights into mechanisms underlying the rapid decay of its active, signaling state.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Ultrafast transient absorption spectra and kinetics of human blue cone visual pigment at room temperature.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- In-silico predicted mouse melanopsins with blue spectral shifts deliver efficient subcellular signaling.Cell communication and signaling : CCS · 2024Article
- Structure network-based landscape of rhodopsin misfolding by mutations and algorithmic prediction of small chaperone action.Computational and structural biotechnology journal · 2021Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human color vision is mediated by the red, green, and blue cone visual pigments. Cone opsins are G-protein-coupled receptors consisting of an opsin apoprotein covalently linked to the 11-cis-retinal chromophore. All visual pigments share a common evolutionary origin, and red and green cone opsins exhibit a higher homology, whereas blue cone opsin shows more resemblance to the dim light receptor rhodopsin. Here we show that chromophore regeneration in photoactivated blue cone opsin exhibits intermediate transient conformations and a secondary retinoid binding event with slower binding kinetics. We also detected a fine-tuning of the conformational change in the photoactivated blue cone opsin binding site that alters the retinal isomer binding specificity. Furthermore, the molecular models of active and inactive blue cone opsins show specific molecular interactions in the retinal binding site that are not present in other opsins. These findings highlight the differential conformational versatility of human cone opsin pigments in the chromophore regeneration process, particularly compared to rhodopsin, and point to relevant functional, unexpected roles other than spectral tuning for the cone visual pigments.
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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.