Key Laboratory of Industrial Fermentation (Ministry of Education), Hubei University of Technology, Wuhan, China.
Hubei Key Laboratory of Industrial Microbiology, Hubei University of Technology, Wuhan, China.
J Biomol Struct Dyn. 2020 Oct;38(16):4883-4894. doi: 10.1080/07391102.2019.1692073. Epub 2019 Nov 19.
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are abundant in all species. They play critical roles in many cellular processes, including transcription/translation regulation, cell cycle regulation, mRNA processing, scaffolding, apoptosis, and assembly of large protein complexes or membraneless organelles. IDPs/IDRs usually recognize their biological targets via short recognition segments. Although the recognition segments are enriched in hydrophobic residues and IDPs/IDRs rely on hydrophobic contacts to interact with their targets, charged residues are also frequently observed within the recognition segments, particularly in those forming α-helix in the complex structure. By summarizing recent studies, this review aims to present the roles of electrostatic interactions played in the molecular recognition processes of IDPs/IDRs. In particular, we discuss how electrostatic interactions modulate the molecular recognition mechanisms and how charge patterning modulates the functions of IDPs/IDRs. Roles of electrostatic interactions in liquid-liquid phase separation are also discussed.Communicated by Ramaswamy H. Sarma.
无规蛋白（IDPs）和无规区域（IDRs）在所有物种中都很丰富。它们在许多细胞过程中发挥着关键作用，包括转录/翻译调控、细胞周期调控、mRNA 处理、支架、细胞凋亡以及大蛋白复合物或无膜细胞器的组装。IDPs/IDRs 通常通过短的识别片段来识别其生物靶标。尽管识别片段富含疏水性残基，并且 IDPs/IDRs 依赖疏水性接触来与靶标相互作用，但在识别片段中也经常观察到带电残基，特别是在形成复合物结构中α-螺旋的那些片段中。通过总结最近的研究，本综述旨在介绍静电相互作用在 IDPs/IDRs 的分子识别过程中所起的作用。特别是，我们讨论了静电相互作用如何调节分子识别机制，以及电荷模式如何调节 IDPs/IDRs 的功能。还讨论了静电相互作用在液-液相分离中的作用。由 Ramaswamy H. Sarma 交流。
