Order/Disorder Transitions Upon Protein Binding: A Unifying Perspective.

IF 4.3 3区 材料科学 Q1 ENGINEERING, ELECTRICAL & ELECTRONIC ACS Applied Electronic Materials Pub Date : 2024-12-01 Epub Date: 2024-08-19 DOI:10.1002/prot.26737
Olga O Lebedenko, Ashok Sekhar, Nikolai R Skrynnikov
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Abstract

When two proteins bind to each other, this process is often accompanied by a change in their structural states (from disordered to ordered or vice versa). As it turns out, there are 10 distinct possibilities for such binding-related order/disorder transitions. Out of this number, seven scenarios have been experimentally observed, while another three remain hitherto unreported. As an example, we discuss the so-called mutual synergistic folding, whereby two disordered proteins come together to form a fully structured complex. Our bioinformatics analysis of the Protein Databank found potential new examples of this remarkable binding mechanism.

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蛋白质结合时的有序/无序转变:统一的视角
当两种蛋白质相互结合时,这一过程往往伴随着它们结构状态的改变(从无序到有序或相反)。事实证明,这种与结合相关的有序/无序转变有 10 种不同的可能性。在这10种可能性中,有7种已被实验观察到,而另外3种至今仍未被报道。作为一个例子,我们讨论了所谓的相互协同折叠,即两个无序蛋白质结合在一起形成一个结构完整的复合物。我们对蛋白质数据库(Protein Databank)进行了生物信息学分析,发现了这种非凡结合机制的潜在新实例。
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来源期刊
CiteScore
7.20
自引率
4.30%
发文量
567
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