Illuminating the molecular basis of human daylight vision

Photopic vision, including fast motion and color perception in daylight, is mediated by cone opsins, specialized G protein-coupled receptors (GPCRs). Despite sharing the same chromophore, the three receptor subtypes absorb light at different wavelengths of the visible spectrum. The molecular mechanisms governing their spectral properties and exceptionally rapid responses remain largely unknown. We report cryo-electron microscopy structures of the human blue-sensitive (OPN1SW) and green-sensitive (OPN1MW) cone opsins in their dark-adapted states, combined with femtosecond-resolution spectroscopy, functional assays, and advanced simulations. The data reveal distinct chromophore stabilization mechanisms across human visual opsins and specific sequence adaptations in the GPCR microswitch motifs, underlining their structural plasticity and distinct activation mechanisms. These findings delineate the molecular basis of the evolutionary refinements fulfilling the needs of vision in daylight.

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Publication Details

Journal
Science
Published
2026-06-25
DOI
https://doi.org/10.1126/science.adz3624
Primary Topic
Retinal Development and Disorders
Type
article
Field-Weighted Citation Impact
0.00

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article

Illuminating the molecular basis of human daylight vision

Asato Kojima, Andrej Hovan, Jakub Dostál, Martin V. Appleby et al.
Science
Retinal Development and Disorders
article

Illuminating the molecular basis of human daylight vision

Asato Kojima, Andrej Hovan, Jakub Dostál, Martin V. Appleby, Saumik Sen, Miroslav Kloz, Deborah Walter, Gebhard F. X. Schertler, Polina Isaikina, John H. Beale, Hideaki Kato, Sarah L. Schmidt
article en

Abstract

Photopic vision, including fast motion and color perception in daylight, is mediated by cone opsins, specialized G protein-coupled receptors (GPCRs). Despite sharing the same chromophore, the three receptor subtypes absorb light at different wavelengths of the visible spectrum. The molecular mechanisms governing their spectral properties and exceptionally rapid responses remain largely unknown. We report cryo-electron microscopy structures of the human blue-sensitive (OPN1SW) and green-sensitive (OPN1MW) cone opsins in their dark-adapted states, combined with femtosecond-resolution spectroscopy, functional assays, and advanced simulations. The data reveal distinct chromophore stabilization mechanisms across human visual opsins and specific sequence adaptations in the GPCR microswitch motifs, underlining their structural plasticity and distinct activation mechanisms. These findings delineate the molecular basis of the evolutionary refinements fulfilling the needs of vision in daylight.

ScienceVol. 392(6805)
SIB Swiss Institute of Bioinformatics (CH), Tokyo University of the Arts (JP), University of Zurich (CH), Paul Scherrer Institute (CH), ETH Zurich (CH), Japan Science and Technology Agency (JP), Extreme Light Infrastructure Beamlines (CZ), The University of Tokyo (JP)
Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung, Grantová Agentura České Republiky, Horizon 2020 Framework Programme, European Research Council, Japan Science and Technology Agency, Core Research for Evolutional Science and Technology
Openalex Percentile: Top 11%
Retinal Development and Disorders
DOIOpen Access PDFOpenAlex
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