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首页> 外文期刊>Journal of Molecular Biology >Backbone dynamics of a cbEGF domain pair in the presence of calcium.
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Backbone dynamics of a cbEGF domain pair in the presence of calcium.

机译：钙存在下cbEGF域对的骨干动力学。

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摘要

Calcium binding (cb) epidermal growth factor-like (EGF) domains are found in a wide variety of extracellular proteins with diverse functions. In several proteins, including the fibrillins (1 and 2), the low-density lipoprotein receptor, the Notch receptor and related molecules, these domains are organised as multiple tandem repeats. The functional importance of calcium-binding by EGF domains has been underscored by the identification of missense mutations associated with defective calcium-binding, which have been linked to human diseases. Here, we present (15)N backbone relaxation data for a pair of cbEGF domains from fibrillin-1, the defective protein in the Marfan syndrome. The data were best fit using a symmetric top model, confirming the extended conformation of the cbEGF domain pair. Our data demonstrate that calcium plays a key role in stabilising the rigidity of the domain pair on the pico- to millisecond time-scale. Strikingly, the most dynamically stable region of the construct is centred about the domain interface. These results provide important insight into the properties of intact fibrillin-1, the consequences of Marfan syndrome causing mutations, and the ultrastructure of fibrillins and other extracellular matrix proteins. Copyright 2000 Academic Press.
机译：钙结合（cb）表皮生长因子样（EGF）结构域存在于多种功能多样的细胞外蛋白中。在几种蛋白中，包括原纤维蛋白（1和2），低密度脂蛋白受体，Notch受体和相关分子，这些结构域被组织为多个串联重复序列。通过鉴定与有缺陷的钙结合有关的错义突变，已强调了EGF结构域与钙结合的功能重要性，这种错义突变与人类疾病有关。在这里，我们提出了来自原纤维蛋白-1（马凡氏综合征中的缺陷蛋白）的一对cbEGF域的（15）N骨架弛豫数据。使用对称顶部模型对数据进行最佳拟合，证实了cbEGF域对的扩展构象。我们的数据表明，钙在皮秒至毫秒级时域中稳定畴对的刚性中起着关键作用。引人注目的是，构造的最动态稳定区域以域接口为中心。这些结果为完整的原纤维蛋白-1的特性，马凡氏综合征引起突变的后果以及原纤维蛋白和其他细胞外基质蛋白的超微结构提供了重要的见识。版权所有2000学术出版社。

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