Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104, United States.
Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104, United States; Biochemistry & Molecular Biophysics Graduate Group, University of Pennsylvania, Philadelphia, PA 19104, United States.
Curr Opin Struct Biol. 2018 Apr;49:36-43. doi: 10.1016/j.sbi.2017.12.007. Epub 2018 Jan 4.
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.
无规则蛋白（IDPs）在多种细胞功能中起着关键作用。相关的是，它们是大分子复合物的组成部分，其构象灵活性有助于调节与结合伙伴的相互作用。IDPs 通常通过短序列基序与其结合伙伴相互作用，这些基序在无规则区域内经常重复。因此，多价相互作用在大分子复合物中的 IDPs 和它们的结合伙伴中很常见。在这里，我们将讨论 IDP 多价性在三个非常不同的大分子组装体中的重要性：生物分子凝聚物、核孔和细胞骨架。
