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蛋白质结合时的有序-无序转变:一个统一的视角。

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

机构信息

Laboratory of Biomolecular NMR, St. Petersburg State University, St. Petersburg, Russia.

Molecular Biophysics Unit, Indian Institute of Science Bangalore, Bengaluru, India.

出版信息

Proteins. 2024 Dec;92(12):1459-1463. doi: 10.1002/prot.26737. Epub 2024 Aug 19.

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.

摘要

当两个蛋白质相互结合时,这个过程通常伴随着它们结构状态的变化(从无序到有序,或者相反)。事实证明,这种结合相关的有序/无序转变有 10 种不同的可能性。在这个数字中,有七种情况已经被实验观察到,而另外三种情况迄今为止尚未报道。例如,我们讨论了所谓的相互协同折叠,即两个无序的蛋白质聚集在一起形成一个完全结构的复合物。我们对蛋白质数据库的生物信息学分析发现了这种显著结合机制的潜在新例子。

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