Uversky Vladimir N
From the Department of Molecular Medicine, USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, Florida 33612, the Biological Sciences Department, Faculty of Science, King Abdulaziz University, Jeddah 21589, Saudi Arabia, the Institute for Biological Instrumentation, Russian Academy of Sciences, 142292 Pushchino, Moscow Region, Russia, and the Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 194064 St. Petersburg, Russian Federation
J Biol Chem. 2016 Mar 25;291(13):6681-8. doi: 10.1074/jbc.R115.685859. Epub 2016 Feb 5.
Biologically active but floppy proteins represent a new reality of modern protein science. These intrinsically disordered proteins (IDPs) and hybrid proteins containing ordered and intrinsically disordered protein regions (IDPRs) constitute a noticeable part of any given proteome. Functionally, they complement ordered proteins, and their conformational flexibility and structural plasticity allow them to perform impossible tricks and be engaged in biological activities that are inaccessible to well folded proteins with their unique structures. The major goals of this minireview are to show that, despite their simplified amino acid sequences, IDPs/IDPRs are complex entities often resembling chaotic systems, are structurally and functionally heterogeneous, and can be considered an important part of the structure-function continuum. Furthermore, IDPs/IDPRs are everywhere, and are ubiquitously engaged in various interactions characterized by a wide spectrum of binding scenarios and an even wider spectrum of structural and functional outputs.
具有生物活性但结构松散的蛋白质代表了现代蛋白质科学的一个新领域。这些内在无序蛋白质(IDP)以及包含有序和内在无序蛋白质区域(IDPR)的杂合蛋白质在任何给定的蛋白质组中都占据显著比例。在功能上,它们补充了有序蛋白质的功能,其构象灵活性和结构可塑性使它们能够施展不可思议的技巧,并参与具有独特结构的折叠良好的蛋白质所无法进行的生物活动。本综述的主要目的是表明,尽管IDP/IDPR的氨基酸序列简单,但它们是复杂的实体,常常类似于混沌系统,在结构和功能上具有异质性,并且可以被视为结构-功能连续体的重要组成部分。此外,IDP/IDPR无处不在,广泛参与各种相互作用,这些相互作用具有广泛的结合模式以及更加广泛的结构和功能输出。