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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Structure and function in rhodopsin: Further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function
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Structure and function in rhodopsin: Further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function

机译：视紫红质的结构和功能：进一步阐明了盘内半胱氨酸Cys-110，-185和-187在视紫红质折叠和功能中的作用

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摘要

The disulfide bond between Cys-110 and Cys-187 in the intradiscal domain is required for correct folding in vivo and function of mammalian rhodopsin. Misfolding in rhodopsin, characterized by the loss of ability to bind ll-cis-retinal, has been shown to be caused by an intradiscal disulfide bond different from the above native disulfide bond. Further, naturally occurring single mutations of the intradiscal cysteines (Cll0F, Cll0Y, and C187Y) are associated with retinitis pigmentosa (RP). To elucidate fur ther the role of every one of the three intradiscal cysteines, mutants containing single-cysteine replacements by alanine residues and the above three RP mutants have been studied. We find that Cll0A, Cll0F, and Cll0Y all form a disulfide bond between C185 and C187 and cause loss of retinal binding. C185A allows the formation of a Cll0-C187 disulfide bond, with wild-type-like rhodopsin phenotype. C187A forms a disulfide bond between Cllo and C185 and binds retinal, and the pigment formed has markedly altered bleaching behavior. However, the opsin from the RP mutant C187Y forms no rhodopsin chromophore.
机译：在椎间盘内域中Cys-110和Cys-187之间的二硫键是哺乳动物视紫红质在体内正确折叠和功能所必需的。视紫红质的错误折叠，其特征在于失去结合II-顺-视黄醛的能力，已被证明是由不同于上述天然二硫键的盘内二硫键引起的。此外，盘内半胱氨酸的自然发生的单一突变（C110F，C110Y和C187Y）与色素性视网膜炎（RP）有关。为了进一步阐明三个盘内半胱氨酸中的每一个的作用，已经研究了含有被丙氨酸残基单半胱氨酸替代的突变体和上述三个RP突变体。我们发现Cll0A，Cll0F和Cll0Y都在C185和C187之间形成二硫键，并导致视网膜结合丧失。 C185A允许形成具有野生型视紫红质表型的C110-C187二硫键。 C187A在Cllo和C185之间形成二硫键并结合视网膜，并且形成的颜料具有显着改变的漂白行为。然而，来自RP突变体C187Y的视蛋白不形成视紫红质生色团。

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