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首页> 外文期刊>Biochemistry >Cold Shock Domain of the Human Y-Box Protein YB-1.Backbone Dynamics and Equilibrium between the Native State and a Partially Unfolded State
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Cold Shock Domain of the Human Y-Box Protein YB-1.Backbone Dynamics and Equilibrium between the Native State and a Partially Unfolded State

机译：人类Y盒蛋白YB-1的冷激域。原始状态和部分展开状态之间的骨干动力学和平衡

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摘要

The three-dimensional structure of the central cold shock domain (CSD) of the human Y-box protein (YB-1 CSD) is virtually identical to those available for the bacterial cold shock proteins (Csp's).We have further characterized YB-1 CSD by studying its dynamics by nuclear magnetic resonance.The observed structural similarity is reflected in the backbone dynamics,which for YB-1 CSD is very similar to that of the Escherichia coli protein CspA.The rotational correlation time of YB-1 CSD shows that it is a monomer.This indicates that the dimerization observed for the YB-1 protein is not caused by its CSD,but involves other parts of this protein.The YB-1 CSD is only marginally stable as are the mesophilic bacterial Csp's.In contrast to the rapid two-state folding of the bacterial Csp's,the formation of the native form of YB-1 CSD is slow and at least a three-state process.The NMR experiments revealed the presence of a second state of YB-1 CSD in equilibrium with the native form.The exchange rates from and to the folded state are in the order of 0.2 and 0.5 s~(-1),respectively.Relaxation experiments indicated that the second state is a highly flexible,partly structured molecule.
机译：人Y盒蛋白（YB-1 CSD）中央冷激域（CSD）的三维结构实际上与细菌冷激蛋白（Csp's）的三维结构相同。我们进一步表征了YB-1通过核磁共振研究CSD的动力学，观察到的结构相似性反映在骨架动力学上，YB-1 CSD与大肠杆菌CspA非常相似.YB-1 CSD的旋转相关时间表明：这表示它是单体。这表明YB-1蛋白的二聚化不是由其CSD引起的，而是涉及该蛋白的其他部分.YB-1 CSD与嗜温细菌Csp一样仅略微稳定。细菌Csp的快速两态折叠导致天然形式的YB-1 CSD形成缓慢且至少处于三态过程。NMR实验表明，YB-1 CSD处于第二态。与自然形态的平衡从松弛状态到折叠状态的速率分别为0.2和0.5 s〜（-1）。松弛实验表明，第二状态是高度柔性的，部分结构化的分子。

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