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Conditionally and Transiently Disordered Proteins: Awakening Cryptic Disorder To Regulate Protein Function

机译:有条件和暂时紊乱的蛋白质:唤醒隐匿性疾病以调节蛋白质功能

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摘要

Proteins, with their seemingly limitless functional diversity, are major players in the maintenance of life. The ability of proteins to fulfill these various biological functions is encoded in their amino acid sequences. Although for a very long time it has been believed that the specific functionality of a given protein is predetermined by its unique three-dimensional (3-D) structure, it is recognized now that a large portion of any given proteome is occupied by so-called intrinsically disordered proteins (IDPs). These proteins and others with disordered regions (IDPRs) possess a very wide range of biological functions, but are characterized by the lack of a well-defined 3-D structure under physiological conditions. Some illustrative biological activities of IDPs include regulation of cell division, transcription and translation, signal transduction, protein phosphorylation and other post-translational modifications, storage of small molecules, chaperone action, and regulation of the self-assembly of large multiprotein complexes such as the ribosome. For IDPs, structural flexibility and plasticity originating from their lack of a definite ordered 3-D structure represent a major functional advantage, enabling them to interact with a broad range of binding partners including other proteins, peptides, membranes, nucleic acids, oligonucleotides, oligosaccharides, and various small molecules.
机译:蛋白质,看似无限的功能多样性,是维持生命的主要参与者。蛋白质实现这些各种生物学功能的能力在其氨基酸序列中编码。尽管很长一段时间以来,人们一直认为给定蛋白质的特定功能是由其独特的三维(3-D)结构预先确定的,但是现在人们已经认识到,给定蛋白质组的很大一部分都被蛋白质占据了,称为内在无序蛋白(IDP)。这些蛋白质和其他具有无序区域(IDPR)的蛋白质具有非常广泛的生物学功能,但其特征是在生理条件下缺乏明确的3-D结构。 IDP的一些示例性生物学活性包括调节细胞分裂,转录和翻译,信号转导,蛋白质磷酸化和其他翻译后修饰,小分子的存储,分子伴侣的作用以及调节大型多蛋白复合物(如蛋白质)的自组装。核糖体。对于IDP,由于缺乏明确的有序3-D结构而产生的结构灵活性和可塑性代表了主要的功能优势,使它们能够与广泛的结合伴侣相互作用,包括其他蛋白质,肽,膜,核酸,寡核苷酸,寡糖以及各种小分子。

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