从序列和力到结构、功能和无规则蛋白质的进化。
From sequence and forces to structure, function, and evolution of intrinsically disordered proteins.
机构信息
Molecular Structure and Function, Hospital for Sick Children, Toronto, ON, M5G 1X8, Canada; Department of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada.
出版信息
Structure. 2013 Sep 3;21(9):1492-9. doi: 10.1016/j.str.2013.08.001.
Intrinsically disordered proteins (IDPs), which lack persistent structure, are a challenge to structural biology due to the inapplicability of standard methods for characterization of folded proteins as well as their deviation from the dominant structure/function paradigm. Their widespread presence and involvement in biological function, however, has spurred the growing acceptance of the importance of IDPs and the development of new tools for studying their structure, dynamics, and function. The interplay of folded and disordered domains or regions for function and the existence of a continuum of protein states with respect to conformational energetics, motional timescales, and compactness are shaping a unified understanding of structure-dynamics-disorder/function relationships. In the 20(th) anniversary of Structure, we provide a historical perspective on the investigation of IDPs and summarize the sequence features and physical forces that underlie their unique structural, functional, and evolutionary properties.
无规卷曲蛋白质（IDPs）缺乏持久结构，这对结构生物学来说是一个挑战，因为标准的折叠蛋白质特征描述方法并不适用，而且它们也偏离了主要的结构/功能范式。然而，它们广泛存在并参与生物功能，这促使人们越来越认识到 IDPs 的重要性，并开发了新的工具来研究它们的结构、动态和功能。折叠和无规结构域或区域在功能上的相互作用以及在构象能、运动时间尺度和紧凑性方面存在蛋白质状态的连续统，正在形成对结构-动力学-无序/功能关系的统一理解。在《结构》创刊 20 周年之际，我们提供了对 IDPs 研究的历史视角，并总结了构成其独特结构、功能和进化特性的序列特征和物理力。
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