Department of Molecular Medicine, USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA and Laboratory of New Methods in Biology, Institute for Biological Instrumentation, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia.
Brief Funct Genomics. 2020 Jan 22;19(1):60-68. doi: 10.1093/bfgp/ely023.
Although for more than a century a protein function was intimately associated with the presence of unique structure in a protein molecule, recent years witnessed a skyrocket rise of the appreciation of protein intrinsic disorder concept that emphasizes the importance of the biologically active proteins without ordered structures. In different proteins, the depth and breadth of disorder penetrance are different, generating an amusing spatiotemporal heterogeneity of intrinsically disordered proteins (IDPs) and intrinsically disordered protein region regions (IDPRs), which are typically described as highly dynamic ensembles of rapidly interconverting conformations (or a multitude of short lifetime structures). IDPs/IDPRs constitute a substantial part of protein kingdom and have unique functions complementary to functional repertoires of ordered proteins. They are recognized as interaction specialists and global controllers that play crucial roles in regulation of functions of their binding partners and in controlling large biological networks. IDPs/IDPRs are characterized by immense binding promiscuity and are able to use a broad spectrum of binding modes, often resulting in the formation of short lifetime complexes. In their turn, functions of IDPs and IDPRs are controlled by various means, such as numerous posttranslational modifications and alternative splicing. Some of the functions of IDPs/IDPRs are briefly considered in this review to shed some light on the biological roles of short-lived structures at large.
虽然一个多世纪以来，蛋白质的功能都与蛋白质分子中独特结构的存在密切相关，但近年来，人们对蛋白质固有无序概念的认识迅速提高，这一概念强调了具有生物活性但没有有序结构的蛋白质的重要性。在不同的蛋白质中，无序的深度和广度不同，产生了有趣的固有无序蛋白质（IDP）和固有无序蛋白质区域（IDPR）的时空异质性，这些蛋白质通常被描述为快速相互转化构象的高度动态集合（或多种短寿命结构）。IDP/IDPR 构成了蛋白质王国的重要组成部分，具有与有序蛋白质功能谱互补的独特功能。它们被认为是相互作用的专家和全局控制器，在调节其结合伙伴的功能和控制大型生物网络方面发挥着关键作用。IDP/IDPR 具有巨大的结合混杂性，并能够使用广泛的结合模式，通常导致短寿命复合物的形成。反过来，IDP 和 IDPR 的功能受到多种翻译后修饰和选择性剪接等各种方式的控制。本文简要讨论了 IDP/IDPR 的一些功能，以期阐明短寿命结构在更大范围内的生物学作用。
