ArticleProceedings of the National Academy of Sciences of the United States of America2025
Structure of human green cone opsin yields insights into mechanisms underlying the rapid decay of its active, signaling state.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed.
- E122Q rhodopsin: pigment microspectrophotometry, photoreceptor light responses, and bleaching adaptation.Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology · 2026Article
- Biophysical and structural analysis of human green cone opsin.Biophysical journal · 2026Article
- Optoretinography in R9AP-bradyopsia reveals the essential role of G-protein signaling in the human cone elongation response.bioRxiv : the preprint server for biology · 2026Article
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3 authors.
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Abstract
Cone opsins enable daylight vision and color discrimination. Like their dim-light cousin rhodopsin (Rho) found in rod cells, they use a covalently attached retinal ligand to sense light and initiate visual phototransduction by activating G proteins. Unfortunately, we know less about their structural properties, in part because their activated state is unstable-cone opsins release their retinal agonist within seconds after light activation, ~100× faster than Rho. To determine what causes this rapid release and how it affects G protein activation, we solved the structure of active-state, wild-type human green cone opsin (GCO
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