In Various Protein Complexes, Disordered Protomers Have Large Per-residue Surface Areas and Area of Protein-, DNA- and RNA-binding Interfaces
Document Type
Article
Publication Date
2015
Keywords
Intrinsic disorder, Protein–RNA interaction, Protein–DNA interaction, Protein–protein interaction, Binding surface, Binding interface
Digital Object Identifier (DOI)
https://doi.org/10.1016/j.febslet.2015.08.014
Abstract
We provide first large scale analysis of the peculiarities of surface areas of 5658 dissimilar (below 50% sequence similarity) proteins with known 3D-structures that bind to proteins, DNA or RNAs. We show here that area of the protein surface is highly correlated with the protein length. The size of the interface surface is only modestly correlated with the protein size, except for RNA-binding proteins where larger proteins are characterized by larger interfaces. Disordered proteins with disordered interfaces are characterized by significantly larger per-residue areas of their surfaces and interfaces when compared to the structured proteins. These result are applicable for proteins involved in interaction with DNA, RNA, and proteins and suggest that disordered proteins and binding regions are less compact and more likely to assume extended shape. We demonstrate that disordered protein binding residues in the interfaces of disordered proteins drive the increase in the per residue area of these interfaces. Our results can be used to predict in silico whether a given protomer from the DNA, RNA or protein complex is likely to be disordered in its unbound form.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
FEBS Letters, v. 589, issue 19, p. 2561-2569
Scholar Commons Citation
Wu, Zhonghua; Hu, Gang; Yang, Jianyi; Peng, Zhenling; Uversky, Vladimir N.; and Kurgan, Lukasz, "In Various Protein Complexes, Disordered Protomers Have Large Per-residue Surface Areas and Area of Protein-, DNA- and RNA-binding Interfaces" (2015). Molecular Medicine Faculty Publications. 400.
https://digitalcommons.usf.edu/mme_facpub/400
