Bioinformatics Programming Laboratory, Department of Biotechnology, School of Biosciences and Technology, Vellore Institute of Technology, Vellore 632 014, India.
J Biosci. 2020;45.
Intrinsically disordered proteins (IDPs) are highly flexible and undergo disorder to order transition upon binding. They are highly abundant in human proteomes and play critical roles in cell signaling and regulatory processes. This review mainly focuses on the dynamics of disordered proteins including their conformational heterogeneity, protein-protein interactions, and the phase transition of biomolecular condensates that are central to various biological functions. Besides, the role of RNA-mediated chaperones in protein folding and stability of IDPs were also discussed. Finally, we explored the dynamic binding interface of IDPs as novel therapeutic targets and the effect of small molecules on their interactions.
无规卷曲蛋白质（IDPs）高度灵活，在结合时经历无序到有序的转变。它们在人类蛋白质组中含量丰富，在细胞信号转导和调节过程中发挥关键作用。这篇综述主要关注无规卷曲蛋白质的动力学，包括它们的构象异质性、蛋白质-蛋白质相互作用以及生物分子凝聚物的相变，这些都是各种生物学功能的核心。此外，还讨论了 RNA 介导的伴侣在 IDPs 的折叠和稳定性中的作用。最后，我们探索了 IDPs 的动态结合界面作为新的治疗靶点以及小分子对它们相互作用的影响。
