Functional unfoldomics: Roles of intrinsic disorder in protein (multi)functionality.

3区 生物学 Q1 Biochemistry, Genetics and Molecular Biology
Vladimir N Uversky
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引用次数: 0

Abstract

Intrinsically disordered proteins (IDPs), which are functional proteins without stable tertiary structure, and hybrid proteins containing ordered domains and intrinsically disordered regions (IDRs) constitute prominent parts of all proteomes collectively known as unfoldomes. IDPs/IDRs exist as highly dynamic structural ensembles of rapidly interconverting conformations and are characterized by the exceptional structural heterogeneity, where their different parts are (dis)ordered to different degree, and their overall structure represents a complex mosaic of foldons, inducible foldons, inducible morphing foldons, non-foldons, semifoldons, and even unfoldons. Despite their lack of unique 3D structures, IDPs/IDRs play crucial roles in the control of various biological processes and the regulation of different cellular pathways and are commonly involved in recognition and signaling, indicating that the disorder-based functional repertoire is complementary to the functions of ordered proteins. Furthermore, IDPs/IDRs are frequently multifunctional, and this multifunctionality is defined by their structural flexibility and heterogeneity. Intrinsic disorder phenomenon is at the roots of the structure-function continuum model, where the structure continuum is defined by the presence of differently (dis)ordered regions, and the function continuum arises from the ability of all these differently (dis)ordered parts to have different functions. In their everyday life, IDPs/IDRs utilize a broad spectrum of interaction mechanisms thereby acting as interaction specialists. They are crucial for the biogenesis of numerous proteinaceous membrane-less organelles driven by the liquid-liquid phase separation. This review introduces functional unfoldomics by representing some aspects of the intrinsic disorder-based functionality.

功能展开组学:内在紊乱在蛋白质(多重)功能中的作用。
内在无序蛋白(IDPs)是没有稳定三级结构的功能蛋白,而包含有序结构域和内在无序区(IDRs)的混合蛋白则构成了所有蛋白质组(统称为展开组)的重要组成部分。IDPs/IDRs以快速相互转换构象的高动态结构组合形式存在,其特点是结构异质性极强,不同部分的(无)有序程度不同,整体结构由折叠子、可诱导折叠子、可诱导变形折叠子、非折叠子、半折叠子甚至未折叠子组成,错综复杂。尽管 IDPs/IDRs 缺乏独特的三维结构,但它们在控制各种生物过程和调控不同细胞通路方面发挥着至关重要的作用,并且通常参与识别和信号传递,这表明基于无序的功能剧目与有序蛋白的功能是互补的。此外,IDPs/IDRs 经常具有多功能性,这种多功能性是由其结构的灵活性和异质性决定的。内在无序现象是结构-功能连续体模型的根源,其中结构连续体是由不同(无)序区域的存在所定义的,而功能连续体则产生于所有这些不同(无)序部分具有不同功能的能力。在日常生活中,IDPs/IDRs 利用广泛的相互作用机制,从而成为相互作用专家。在液-液相分离的驱动下,IDPs/IDRs对于众多无膜蛋白质细胞器的生物生成至关重要。本综述通过介绍基于固有无序的功能的某些方面来介绍功能性展开体。
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来源期刊
Advances in protein chemistry and structural biology
Advances in protein chemistry and structural biology BIOCHEMISTRY & MOLECULAR BIOLOGY-
CiteScore
7.40
自引率
0.00%
发文量
66
审稿时长
>12 weeks
期刊介绍: Published continuously since 1944, The Advances in Protein Chemistry and Structural Biology series has been the essential resource for protein chemists. Each volume brings forth new information about protocols and analysis of proteins. Each thematically organized volume is guest edited by leading experts in a broad range of protein-related topics.
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