The multifaceted roles of intrinsic disorder in protein complexes

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• 作者：Vladimir N. Uversky ; ^{vuversky@health.usf.edu" class="auth_mail" title="E-mail the corresponding author}
• 关键词：Intrinsically disordered protein ; Intrinsically disordered protein region ; Protein&ndash ; protein interaction ; Protein complex ; Scaffold ; Regulation ; Polyvalent interaction
• 刊名：FEBS Letters
• 出版年：2015
• 出版时间：14 September 2015
• 年：2015
• 卷：589
• 期：19
• 页码：2498-2506
• 全文大小：2183 K

文摘

Intrinsically disordered proteins (IDPs) and intrinsically disordered protein regions (IDPRs) are important constituents of many protein complexes, playing various structural, functional, and regulatory roles. In such disorder-based protein complexes, functional disorder is used both internally (for assembly, movement, and functional regulation of the different parts of a given complex) and externally (for interactions of a complex with its external regulators). In complex assembly, IDPs/IDPRs serve as the molecular glue that cements complexes or as highly flexible scaffolds. Disorder defines the order of complex assembly and the ability of a protein to be involved in polyvalent interactions. It is at the heart of various binding mechanisms and interaction modes ascribed to IDPs. Disorder in protein complexes is related to multifarious applications of induced folding and induced functional unfolding, or defines the entropic chain activities, such as stochastic machines and binding rheostats. This review opens a FEBS Letters Special Issue on Dynamics, Flexibility, and Intrinsic Disorder in protein assemblies and represents a brief overview of intricate roles played by IDPs and IDPRs in various aspects of protein complexes.