Understanding protein non-folding.
Understanding protein non-folding.
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DOI：
10.1016/j.bbapap.2010.01.017
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发表时间：
2010-06
期刊：
影响因子：
--
通讯作者：
Dunker AK
中科院分区：
文献类型：
--
作者：
Uversky VN;Dunker AK
本文综述了家族的内在无序蛋白质，其成员不能形成刚性的3-D结构在生理条件下，无论是沿着其整个长度或仅在局部区域。相反，这些有趣的蛋白质/区域作为动态集合存在，其中原子位置和骨架Ramachandran角表现出极端的时间波动，而没有特定的平衡值。已知许多这些内在无序的蛋白质执行重要的生物学功能，事实上，这取决于特定的3-D结构的缺乏。这种蛋白质的存在不符合流行的结构-功能范式，该范式认为独特的3-D结构是功能的先决条件。因此，蛋白质结构-功能范式必须扩展到包括内在无序的蛋白质和蛋白质序列，结构和功能之间的替代关系。这一范式的转变代表了生物化学、生物物理学和分子生物学的重大突破，因为它开启了对蛋白质复杂生命的新的理解水平。本文将试图回答以下问题：内在无序蛋白质是如何被发现的？为什么这些蛋白质不折叠？内在障碍有什么特别之处？无序蛋白质/区域的功能优势是什么？这些蛋白质的功能是什么？内在无序蛋白质与人类疾病之间的关系是什么？
This review describes the family of intrinsically disordered proteins, members of which fail to form rigid 3-D structures under physiological conditions, either along their entire lengths or only in localized regions. Instead, these intriguing proteins/regions exist as dynamic ensembles within which atom positions and backbone Ramachandran angles exhibit extreme temporal fluctuations without specific equilibrium values. Many of these intrinsically disordered proteins are known to carry out important biological functions which, in fact, depend on the absence of specific 3-D structure. The existence of such proteins does not fit the prevailing structure-function paradigm, which states that unique 3-D structure is a prerequisite to function. Thus, the protein structure-function paradigm has to be expanded to include intrinsically disordered proteins and alternative relationships among protein sequence, structure, and function. This shift in the paradigm represents a major breakthrough for biochemistry, biophysics and molecular biology, as it opens new levels of understanding with regard to the complex life of proteins. This review will try to answer the following questions: How were intrinsically disordered proteins discovered? Why don't these proteins fold? What is so special about intrinsic disorder? What are the functional advantages of disordered proteins/regions? What is the functional repertoire of these proteins? What are the relationships between intrinsically disordered proteins and human diseases?
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