Roles of intrinsic disorder in protein-nucleic acid interactions.
Roles of intrinsic disorder in protein-nucleic acid interactions.
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DOI：
10.1039/c1mb05258f
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发表时间：
2012-01
影响因子：
--
通讯作者：
Dyson HJ
中科院分区：
文献类型：
--
作者：
Dyson HJ
蛋白质和核酸之间的相互作用代表了无序段，接头，尾巴和其他实体在复合物功能中的作用，这些功能必须具有高亲和力和特异性，但在不再需要时必须能够解离。文献一直是无序蛋白与其他蛋白质的相互作用，在核酸（部分RNA）中也经常观察到疾病，而在相互作用的蛋白质中也经常观察到。与它们相互作用。相比之下，在自由状态下，诱发的RNA - 蛋白质相互作用已被认可了很多年 - 这种现象的存在和普遍性提供了最明显的RNA及其与蛋白质相互作用的证据必须被视为高度动态，RNA的动态性质及其折叠和展开状态的多样性是其性质和功能的组成部分。
Interactions between proteins and nucleic acids typify the role of disordered segments, linkers, tails and other entities in the function of complexes that must form with high affinity and specificity but which must be capable of dissociating when no longer needed. While much of the emphasis in the literature has been on the interactions of disordered proteins with other proteins, disorder is also frequently observed in nucleic acids (particularly RNA) and in the proteins that interact with them. The interactions of disordered proteins with DNA most often manifest as molding of the protein onto the B-form DNA structure, although some well-known instances involve remodeling of the DNA structure that seems to require that the interacting proteins be disordered to various extents in the free state. By contrast, induced fit in RNA-protein interactions has been recognized for many years – the existence and prevalence of this phenomenon provides the clearest possible evidence that RNA and its interactions with proteins must be considered as highly dynamic, and the dynamic nature of RNA and its multiplicity of folded and unfolded states is an integral part of its nature and function.
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影响因子：
11.4
作者：
Allain, FHT;Yen, YM;Feigon, J
通讯作者：
Feigon, J
影响因子：
6.1
作者：
Dyson, H. Jane
通讯作者：
Dyson, H. Jane
DOI：
10.1073/pnas.0805050105
发表时间：
2008-09-16
影响因子：
11.1
作者：
Doucleff, Michaeleen;Clore, G. Marius
通讯作者：
Clore, G. Marius
影响因子：
64.8
作者：
Felsenfeld, G;Groudine, M
通讯作者：
Groudine, M
影响因子：
5.6
作者：
Gearhart, MD;Holmbeck, SMA;Wright, PE
通讯作者：
Wright, PE