Multivalent IDP assemblies: Unique properties of LC8-associated, IDP duplex scaffolds.

Multivalent IDP assemblies: Unique properties of LC8-associated, IDP duplex scaffolds.
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DOI:
10.1016/j.febslet.2015.07.032
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发表时间:
2015-09-14
期刊:
影响因子:
3.5
通讯作者:
Barbar E
Barbar E
中科院分区:
生物学3区
文献类型:
--
作者:
Clark SA;Jespersen N;Woodward C;Barbar E

文献摘要

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各种各样的亚细胞复合物由一个或多个固有无序蛋白(IDP)组成,这些蛋白是多价的,柔性的,并且以不同伴侣蛋白的动态结合为特征。这些多价IDP组件,广泛的功能多样性,在这里分为五个类别区分IDP链的数量和伴侣蛋白在功能复合物的安排。每一类的例子都结合国内流离失所者特殊的分子和生物特性加以概述。详细考虑了一种类型- IDP双链支架。其独特的功能包括两个IDP链的平行排列,形成新的自相关结构域,增强对其他二价配体的亲和力,以及枢纽蛋白LC 8的普遍结合。对于两个IDP双链体支架,动力蛋白中间链IC和核孔蛋白Nup 159,这些双链体特征以及IDP的固有灵活性对其组装和功能至关重要。一种新型的IDP-LC 8相互作用,分布在多个IDP识别位点之间的LC 8的结合,描述了Nup 159组装。
A wide variety of subcellular complexes are composed of one or more intrinsically disordered proteins (IDPs) that are multivalent, flexible, and characterized by dynamic binding of diverse partner proteins. These multivalent IDP assemblies, of broad functional diversity, are classified here into five categories distinguished by the number of IDP chains and the arrangement of partner proteins in the functional complex. Examples of each category are summarized in the context of the exceptional molecular and biological properties of IDPs. One type – IDP duplex scaffolds – is considered in detail. Its unique features include parallel alignment of two IDP chains, formation of new self-associated domains, enhanced affinity for additional bivalent ligands, and ubiquitous binding of the hub protein LC8. For two IDP duplex scaffolds, dynein intermediate chain IC and nucleoporin Nup159, these duplex features, together with the inherent flexibility of IDPs, are central to their assembly and function. A new type of IDP-LC8 interaction, distributed binding of LC8 among multiple IDP recognition sites, is described for Nup159 assembly.