ArticleThe Journal of biological chemistry2015
Conformational selection and equilibrium governs the ability of retinals to bind opsin.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 28 citations in OpenAlex.
- Biophysical and structural analysis of human green cone opsin.Biophysical journal · 2026Article
- A rapid, tag-free way to purify functional GPCRs.The Journal of biological chemistry · 2024Article
- Adaptation of Antarctic Icefish Vision to Extreme Environments.Molecular biology and evolution · 2023Article
- Chromenone derivatives as novel pharmacological chaperones for retinitis pigmentosa-linked rod opsin mutants.Human molecular genetics · 2022Article
- Ancient whale rhodopsin reconstructs dim-light vision over a major evolutionary transition: Implications for ancestral diving behavior.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- FRET sensors reveal the retinal entry pathway in the G protein-coupled receptor rhodopsin.iScience · 2022Article
- Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.Frontiers in chemistry · 2022Review
- Novel fluorescent GPCR biosensor detects retinal equilibrium binding to opsin and active G protein and arrestin signaling conformations.The Journal of biological chemistry · 2020Article
- Activation Microswitches in Adenosine Receptor ABiochemistry · 2020Article
- Structural Model of Ghrelin Bound to its G Protein-Coupled Receptor.Structure (London, England : 1993) · 2019Article
- Article
- 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
- Decay of an active GPCR: Conformational dynamics govern agonist rebinding and persistence of an active, yet empty, receptor state.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Activation of the A2A adenosine G-protein-coupled receptor by conformational selection.Nature · 2016Article
- Beyond spectral tuning: human cone visual pigments adopt different transient conformations for chromophore regeneration.Cellular and molecular life sciences : CMLS · 2016Article
- Structural dynamics and energetics underlying allosteric inactivation of the cannabinoid receptor CB1.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Despite extensive study, how retinal enters and exits the visual G protein-coupled receptor rhodopsin remains unclear. One clue may lie in two openings between transmembrane helix 1 (TM1) and TM7 and between TM5 and TM6 in the active receptor structure. Recently, retinal has been proposed to enter the inactive apoprotein opsin (ops) through these holes when the receptor transiently adopts the active opsin conformation (ops*). Here, we directly test this "transient activation" hypothesis using a fluorescence-based approach to measure rates of retinal binding to samples containing differing relative fractions of ops and ops*. In contrast to what the transient activation hypothesis model would predict, we found that binding for the inverse agonist, 11-cis-retinal (11CR), slowed when the sample contained more ops* (produced using M257Y, a constitutively activating mutation). Interestingly, the increased presence of ops* allowed for binding of the agonist, all-trans-retinal (ATR), whereas WT opsin showed no binding. Shifting the conformational equilibrium toward even more ops* using a G protein peptide mimic (either free in solution or fused to the receptor) accelerated the rate of ATR binding and slowed 11CR binding. An arrestin peptide mimic showed little effect on 11CR binding; however, it stabilized opsin · ATR complexes. The TM5/TM6 hole is apparently not involved in this conformational selection. Increasing its size by mutagenesis did not enable ATR binding but instead slowed 11CR binding, suggesting that it may play a role in trapping 11CR. In summary, our results indicate that conformational selection dictates stable retinal binding, which we propose involves ATR and 11CR binding to different states, the latter a previously unidentified, open-but-inactive conformation.
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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.