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Native Mass Spectrometry Reveals the Simultaneous Binding of Lipids and Zinc to Rhodopsin
International Journal of Mass Spectrometry ( IF 1.8 ) Pub Date : 2021-02-01 , DOI: 10.1016/j.ijms.2020.116477
Carolanne E Norris 1 , James E Keener 1 , Suchithranga M D C Perera 1 , Nipuna Weerasinghe 1 , Steven D E Fried 1 , William C Resager 1 , James G Rohrbough 1 , Michael F Brown 1, 2, 3 , Michael T Marty 1, 3
Affiliation  

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.

中文翻译:

原生质谱法揭示了脂质和锌与视紫红质的同时结合

视紫红质是一种典型的 G 蛋白偶联受体,负责在低光水平下进行窥视。尽管对视紫红质的光活化级联反应非常了解,但仍不清楚脂质和锌如何与受体结合。使用天然质谱,我们开发了一种新的数据分析策略,以解卷积与视紫红质蛋白质结合的锌和脂质,并研究脂质与锌结合之间的变构相互作用。我们发现与视紫红质结合的磷脂酰胆碱比磷脂酰丝氨酸或磷脂酰乙醇胺具有更大的亲和力,并且所有脂质的结合都受锌的影响,但效果不同。相反,锌的结合相对不受脂质的干扰。总体而言,这些数据表明脂质结合可以受到金属离子的强烈和不同的影响。
更新日期:2021-02-01
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