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首页> 外文期刊>Journal of Molecular Biology >Sequential, Structural and Functional Properties of Protein Complexes Are Defined by How Folding and Binding Intertwine
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Sequential, Structural and Functional Properties of Protein Complexes Are Defined by How Folding and Binding Intertwine

机译：蛋白质复合物的顺序，结构和功能性质由折叠和结合交织的方式定义

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Intrinsically disordered proteins (IDPs) fulfill critical biological roles without having the potential to fold on their own. While lacking inherent structure, the majority of IDPs do reach a folded state via interaction with a protein partner, presenting a deep entanglement of the folding and binding processes. Protein disorder has been recognized as a major determinant in several properties of proteins, such as sequence, adopted structure upon binding and function. However, the way the binding process is reflected in these features in general lacks a detailed description. Here, we defined three categories of protein complexes depending on the unbound structural state of the interactors and analyzed them in detail. We found that strikingly, the properties of interactors in terms of sequence and adopted structure are defined not only by the intrinsic structural state of the protein itself but also to a comparable extent by the structural state of the binding partner. The three different types of interactions are also regulated through divergent molecular tactics of post-translational modifications. This not only widens the range of biologically relevant sequence and structure spaces defined by ordered proteins but also presents distinct molecular mechanisms compatible with specific biological processes, separately for each interaction type. The distinct attributes of different binding modes identified in this study can help to understand how various types of interactions serve as building blocks for the assembly of tightly regulated and highly intertwined regulatory networks. (C) 2019 The Authors. Published by Elsevier Ltd.
机译：本质无序的蛋白质（IDP）履行关键的生物角色，而不会潜在地依赖自己。虽然缺乏固有的结构，但大多数IDP通过与蛋白质伴侣的相互作用达到折叠状态，呈现折叠和结合过程的深度纠缠。蛋白质疾病已被认为是在蛋白质的几种性质中的主要决定因素，例如序列，在结合和功能时采用结构。然而，在这些特征中反映了结合过程的方式通常缺乏详细描述。这里，我们根据交流器的未结合结构状态定义了三类蛋白质复合物，并详细分析它们。我们发现，令人惊讶的是，在序列和采用的结构方面的交互式的性质不仅通过蛋白质本身的内在结构状态而是通过结合伴的结构状态而相当的程度。通过翻译后修饰的发散分子策略调节三种不同类型的相互作用。这不仅扩大了由有序蛋白定义的生物学相关序列和结构空间的范围，而且还具有与每个相互作用类型分开的特定生物过程相容的不同分子机制。本研究中鉴定的不同绑定模式的不同属性可以有助于了解各种类型的相互作用是如何用作紧密调节和高度交织的监管网络组装的构建块。 （c）2019年作者。 elsevier有限公司出版

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