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首页> 外文期刊>Biochemistry >Impact of calcium binding and thionylation of S100A1 protein on its nuclear magnetic resonance-derived structure and backbone dynamics
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Impact of calcium binding and thionylation of S100A1 protein on its nuclear magnetic resonance-derived structure and backbone dynamics

机译：S100A1蛋白的钙结合和硫酰化对其核磁共振结构和骨架动力学的影响

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摘要

S100 proteins play a crucial role in multiple important biological processes in vertebrate organisms acting predominantly as calcium signal transmitters. S100A1 is a typical representative of this family of proteins. After four Ca~(2+) ions bind, it undergoes a dramatic conformational change, resulting in exposure, in each of its two identical subunits, a large hydrophobic cleft that binds to target proteins. It has been shown that abnormal expression of S100A1 is strongly correlated with a number of severe human diseases: cardiomyopathy and neurodegenerative disorders. A few years ago, we found that thionylation of Cys 85, the unique cysteine in two identical S100A1 subunits, leads to a drastic increase of the affinity of the protein for calcium. We postulated that the protein activated by thionylation becomes a more efficient calcium signal transmitter. Therefore, we decided to undertake, using nuclear magnetic resonance methods, a comparative study of the structure and dynamics of native and thionylated human S100A1 in its apo and holo states. In this paper, we present the results obtained for both forms of this protein in its holo state and compare them with the previously published structure of native apo-S100. The main conclusion that we draw from these results is that the increased calcium binding affinity of S100A1 upon thionylation arises, most probably, from rearrangement of the hydrophobic core in its apo form.
机译：S100蛋白在主要作为钙信号传递者的脊椎动物中的多个重要生物学过程中起着至关重要的作用。 S100A1是该蛋白家族的典型代表。四个Ca〜（2+）离子结合后，它会发生剧烈的构象变化，从而导致在其两个相同的亚基中都暴露出一个与靶蛋白结合的大疏水裂缝。已经表明，S100A1的异常表达与许多严重的人类疾病密切相关：心肌病和神经退行性疾病。几年前，我们发现Cys 85（两个相同的S100A1亚基中独特的半胱氨酸）的巯基化导致蛋白质与钙的亲和力急剧增加。我们推测，通过巯基化作用激活的蛋白质将成为一种更有效的钙信号传递者。因此，我们决定使用核磁共振方法对自然和硫酰化人S100A1在apo和holo状态下的结构和动力学进行比较研究。在本文中，我们介绍了两种蛋白质在其完整状态下获得的结果，并将它们与天然apo-S100的先前发表的结构进行了比较。我们从这些结果中得出的主要结论是，S100A1硫酰化后钙结合亲和力的增加很可能是由于载脂蛋白形式的疏水核重排而引起的。

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