Intrinsically disordered proteins and biomineralization.
Intrinsically disordered proteins and biomineralization.
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DOI：
10.1016/j.matbio.2016.01.007
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发表时间：
2016-05
期刊：
影响因子：
--
通讯作者：
Villarreal-Ramirez E
中科院分区：
文献类型：
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作者：
Boskey AL;Villarreal-Ramirez E
在脊椎动物和无脊椎动物中，生物矿化是由细胞及其产生的蛋白质控制的。大量这些蛋白质本质上是无序的，当它们与结合伙伴相互作用时获得一些二级结构。这些配对对象包括被沉积的矿物的组成离子、晶体本身、初始晶体形成的模板以及其他本质上无序的蛋白质和多肽。这篇综述推测了为什么内在无序的蛋白质对生物矿化如此重要，并提供了兄弟蛋白(小整合素结合N-糖基化)及其多肽的说明。结论是，柔性的结构和本质上无序的蛋白质与多种表面结合的能力是至关重要的，但关于结合的精确相互作用、能量学和动力学的细节仍有待确定。
In vertebrates and invertebrates biomineralization is controlled by the cell and the proteins they produce. A large number of these proteins are intrinsically disordered, gaining some secondary structure when they interact with their binding partners. These partners include the component ions of the mineral being deposited, the crystals themselves, the template on which the initial crystals form, and other intrinsically disordered proteins and peptides. This review speculates why intrinsically disordered proteins are so important for biomineralization, providing illustrations from the SIBLING (small integrin binding N-glycosylated) proteins and their peptides. It is concluded that the flexible structure, and the ability of the intrinsically disordered proteins to bind to a multitude of surfaces is crucial, but details on the precise-interactions, energetics and kinetics of binding remain to be determined.