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Conservation of Molecular Interactions Stabilizing Bovine and Mouse Rhodopsin

机译：稳定牛和小鼠视紫红质的分子相互作用的守恒。

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摘要

Rhodopsin is the light receptor that initiates phototransduction in rod photoreceptor cells. Thenstructure and function of rhodopsin are tightly linked to molecularinteractionsthatstabilize and determine thenreceptor’s functional state. Single-molecule force spectroscopy (SMFS) was used to localize and quantifymolecularninteractions that structurally stabilize bovine and mouse rhodopsin from native disk membranes of rodnphotoreceptor cells. The mechanical unfolding of bovine and mouse rhodopsin revealed nine major unfoldingnintermediates, each intermediate defining a structurally stable segment in the receptor. These stable structuralnsegments had similar localization and occurrence in both bovine and mouse samples. For each structural segment,nparameters describing their unfolding energy barrier were determined by dynamic SMFS. No major differencesnwere observed between bovine and mouse rhodopsin, thereby implying that the structures of both rhodopsins arenlargely stabilized by similar molecular interactions.
机译：视紫红质是在杆状感光细胞中引发光转导的光受体。然后视紫红质的结构和功能与稳定并决定受体功能状态的分子相互作用紧密相关。使用单分子力谱（SMFS）来定位和量化分子相互作用，该相互作用在结构上稳定了来自杆状感光细胞天然盘膜的牛和鼠视紫红质。牛和鼠视紫红质的机械展开显示出九种主要的展开中间中间体，每个中间体在受体中定义了结构稳定的区段。这些稳定的结构片段在牛和小鼠样品中具有相似的定位和发生。对于每个结构段，通过动态SMFS确定描述其展开能垒的n参数。在牛和小鼠视紫红质之间未观察到主要差异，因此暗示两种视紫红质的结构通过相似的分子相互作用被极大地稳定化。

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  • 来源
    《Biochemistry》 |2010年第49期|p.10412-10420|共9页
  • 作者

    Shiho Kawamura Alejandro T. Colozo Daniel J. Mller and Paul S.-H. Park;

  • 作者单位

    ‡Department of Biosystems Science and Engineering, ETH Z€ urich, 4058 Basel, Switzerland, and §Department of Ophthalmology andVisual Sciences, Case Western Reserve University, Cleveland, Ohio 44106, United States.) Contributed equally to this work;

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