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On the Bioactive Conformation of the Bhodopsin Chromophore: Absolute Sense of Twist around the 6-s-cis Bond

机译:关于视紫红质生色团的生物活性构象:围绕6-s-顺式键的绝对扭曲感。

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摘要

Incubation of opsin with synthetic 6-s-locked retinoids 2a and 2b only led to pigment formation from the alpha-locked 2a, the CD spectrum of which was similar to that of native rhodopsin (Rh). This establishes that the 6-s-bond of the chromophore in rhodopsin is cis, and that its helicity is negative. Earlier cross-linking studies showed that the 11-cis to all-trans photoisomerization occurring in the batho-Rh to lumi-Rh conversion induces a flip over of the side carrying the ring moiety. The GTP-binding assay of pigment Rh-(2a), incorporating retinal analogue 2a, has shown that its activity is 80% that of the native pigment. That is, the overall conformation around the 6-s bond is retained in the steps leading to G-protein activation.
机译:将视蛋白与合成的6-s锁定类视色素2a和2b一起孵育只会导致α锁定的2a形成色素,其CD光谱类似于天然视紫红质(Rh)。这表明视紫红质中发色团的6-s键为顺式,且其螺旋度为负。较早的交联研究表明,在batho-Rh到lumi-Rh转化中发生的11-顺式到全反式光异构化引起了带有环部分的一侧的翻转。结合了视网膜类似物2a的色素Rh-(2a)的GTP结合测定表明,其活性是天然色素的80%。即,在导致G蛋白活化的步骤中保留了6-s键周围的整体构象。

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