Intrinsically disordered regions are often involved in allosteric regulation of multidomain proteins. They can act as disordered linkers to connect and interact with domains, resulting in rather complex allosteric mechanism and novel protein behavior. Therefore, it is necessary to analyze the diverse functions of disordered linkers in order to better understand allostery and relevant regulation process. Here we summarize recent advances in understanding the function of linkers and the advantages of adopting mutlidomain architecture with disorder linkers. It was shown that linkers between domains enhance the local domain concentration and make the allosteric regulation of weakly interacting partners possible, while linkers with only one tethered end cause an entropy effect to reduce binding affinity and prevent aggregation.

中文翻译：

---

具有无序接头的多域蛋白质的变构。

固有无序区域通常参与多域蛋白质的变构调节。它们可以作为无序连接器与域连接和相互作用，导致相当复杂的变构机制和新的蛋白质行为。因此，有必要分析无序连接子的多种功能，以更好地了解变构和相关调控过程。在这里，我们总结了在理解链接器功能方面的最新进展以及采用具有无序链接器的多域架构的优势。结果表明，结构域之间的接头提高了局部结构域的浓度并使弱相互作用伙伴的变构调节成为可能，而只有一个系链末端的接头会引起熵效应以降低结合亲和力并防止聚集。