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• W3110302227 endingPage "116477" @default.
• W3110302227 startingPage "116477" @default.
• W3110302227 abstract "Rhodopsin, a prototypical G-protein-coupled receptor, is responsible for scoptic vision at low-light levels. Although rhodopsin's photoactivation cascade is well understood, it remains unclear how lipid and zinc binding to the receptor are coupled. Using native mass spectrometry, we developed a novel data analysis strategy to deconvolve zinc and lipid bound to the proteoforms of rhodopsin and investigated the allosteric interaction between lipids and zinc binding. We discovered that phosphatidylcholine bound to rhodopsin with a greater affinity than phosphatidylserine or phosphatidylethanolamine, and that binding of all lipids was influenced by zinc but with different effects. In contrast, zinc binding was relatively unperturbed by lipids. Overall, these data reveal that lipid binding can be strongly and differentially influenced by metal ions." @default.
• W3110302227 created "2020-12-07" @default.
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• W3110302227 date "2021-02-01" @default.
• W3110302227 modified "2023-10-18" @default.
• W3110302227 title "Native mass spectrometry reveals the simultaneous binding of lipids and zinc to rhodopsin" @default.
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• W3110302227 doi "https://doi.org/10.1016/j.ijms.2020.116477" @default.
• W3110302227 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7709953" @default.
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