Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar Tudósok krt. 2, H-1117 Budapest, Hungary.
Department of Physiology, Faculty of Medicine, Semmelweis University, Tűzoltó u. 37-47, H-1094 Budapest, Hungary.
Int J Mol Sci. 2018 Oct 26;19(11):3340. doi: 10.3390/ijms19113340.
Intrinsically disordered proteins (IDPs) lack a well-defined 3D structure. Their disordered nature enables them to interact with several other proteins and to fulfil their vital biological roles, in most cases after coupled folding and binding. In this paper, we analyze IDPs involved in a new mechanism, mutual synergistic folding (MSF). These proteins define a new subset of IDPs. Recently we collected information on these complexes and created the Mutual Folding Induced by Binding (MFIB) database. These protein complexes exhibit considerable structural variation, and almost half of them are homodimers, but there is a significant amount of heterodimers and various kinds of oligomers. In order to understand the basic background of the disordered character of the monomers found in MSF complexes, the simplest part of the MFIB database, the homodimers are analyzed here. We conclude that MFIB homodimeric proteins have a larger solvent-accessible main-chain surface area on the contact surface of the subunits, when compared to globular homodimeric proteins. The main driving force of the dimerization is the mutual shielding of the water-accessible backbones and the formation of extra intermolecular interactions.
无规则蛋白质（IDPs）缺乏明确的 3D 结构。它们的无序性质使它们能够与其他几种蛋白质相互作用，并在大多数情况下在折叠和结合后发挥其重要的生物学功能。在本文中，我们分析了参与新机制——相互协同折叠（MSF）的 IDPs。这些蛋白质定义了 IDPs 的一个新子集。最近，我们收集了关于这些复合物的信息，并创建了 Mutual Folding Induced by Binding（MFIB）数据库。这些蛋白质复合物表现出相当大的结构变异，其中近一半是同源二聚体，但也有相当数量的异源二聚体和各种寡聚体。为了了解 MSF 复合物中发现的无序单体的基本背景，我们在这里分析了 MFIB 数据库中最简单的部分，即同源二聚体。我们得出的结论是，与球状同源二聚体蛋白相比，MFIB 同源二聚体蛋白在亚基的接触表面上具有更大的溶剂可及主链表面积。二聚化的主要驱动力是相互屏蔽可及的骨架和形成额外的分子间相互作用。
