The Multifaceted Roles of Intrinsic Disorder in Protein Complexes
Document Type
Article
Publication Date
2015
Keywords
Intrinsically disordered protein, Intrinsically disordered protein region, Protein–protein interaction, Protein complex, Scaffold, Regulation, Polyvalent interaction
Digital Object Identifier (DOI)
https://doi.org/10.1016/j.febslet.2015.06.004
Abstract
Intrinsically disordered proteins (IDPs) and intrinsically disordered protein regions (IDPRs) are important constituents of many protein complexes, playing various structural, functional, and regulatory roles. In such disorder-based protein complexes, functional disorder is used both internally (for assembly, movement, and functional regulation of the different parts of a given complex) and externally (for interactions of a complex with its external regulators). In complex assembly, IDPs/IDPRs serve as the molecular glue that cements complexes or as highly flexible scaffolds. Disorder defines the order of complex assembly and the ability of a protein to be involved in polyvalent interactions. It is at the heart of various binding mechanisms and interaction modes ascribed to IDPs. Disorder in protein complexes is related to multifarious applications of induced folding and induced functional unfolding, or defines the entropic chain activities, such as stochastic machines and binding rheostats. This review opens a FEBS Letters Special Issue on Dynamics, Flexibility, and Intrinsic Disorder in protein assemblies and represents a brief overview of intricate roles played by IDPs and IDPRs in various aspects of protein complexes.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
FEBS Letters, v. 589, issue 19, p. 2498-2506
Scholar Commons Citation
Uversky, Vladimir N., "The Multifaceted Roles of Intrinsic Disorder in Protein Complexes" (2015). Molecular Medicine Faculty Publications. 399.
https://digitalcommons.usf.edu/mme_facpub/399
