IDPs in macromolecular complexes: the roles of multivalent interactions in diverse assemblies.

IDPs in macromolecular complexes: the roles of multivalent interactions in diverse assemblies.
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DOI:
10.1016/j.sbi.2017.12.007
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发表时间:
2018-04
影响因子:
6.8
通讯作者:
Rhoades E
Rhoades E
中科院分区:
生物学2区
文献类型:
--
作者:
Fung HYJ;Birol M;Rhoades E

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内源性无序蛋白(IDPs)在多种细胞功能中起着关键作用。与此相关的是,它们是大分子络合物的组成部分,其中它们的构象灵活性有助于调节与结合伙伴的相互作用。IDPs经常通过短序列基序与其结合伙伴相互作用,这种基序通常在无序区域内重复。因此,在大分子复合体中,IDPs及其结合伙伴的多价相互作用是常见的。在这里,我们讨论了IDP多价性在三个非常不同的大分子组装中的重要性:生物分子凝聚体、核孔和细胞骨架。
Intrinsically disordered proteins (IDPs) have critical roles in a diverse array of cellular functions. Of relevance here is that they are components of macromolecular complexes, where their conformational flexibility helps mediate interactions with binding partners. IDPs often interact with their binding partners through short sequence motifs, commonly repeated within the disordered regions. As such, multivalent interactions are common for IDPs and their binding partners within macromolecular complexes. Here we discuss the importance of IDP multivalency in three very different macromolecular assemblies: biomolecular condensates, the nuclear pore, and the cytoskeleton.
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