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

IF 2.8 4区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Proteins-Structure Function and Bioinformatics Pub Date : 2024-12-01 Epub Date: 2024-08-19 DOI:10.1002/prot.26737

Olga O Lebedenko, Ashok Sekhar, Nikolai R Skrynnikov

引用次数: 0

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。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Proteins-Structure Function and Bioinformatics 生物-生化与分子生物学

CiteScore

5.90

自引率

3.40%

发文量

172

审稿时长

3 months

期刊介绍： PROTEINS : Structure, Function, and Bioinformatics publishes original reports of significant experimental and analytic research in all areas of protein research: structure, function, computation, genetics, and design. The journal encourages reports that present new experimental or computational approaches for interpreting and understanding data from biophysical chemistry, structural studies of proteins and macromolecular assemblies, alterations of protein structure and function engineered through techniques of molecular biology and genetics, functional analyses under physiologic conditions, as well as the interactions of proteins with receptors, nucleic acids, or other specific ligands or substrates. Research in protein and peptide biochemistry directed toward synthesizing or characterizing molecules that simulate aspects of the activity of proteins, or that act as inhibitors of protein function, is also within the scope of PROTEINS. In addition to full-length reports, short communications (usually not more than 4 printed pages) and prediction reports are welcome. Reviews are typically by invitation; authors are encouraged to submit proposed topics for consideration.