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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Wu Z,Hu G,Yang J,Peng Z,Uversky VN,Kurgan Ldoi
10.1016/j.febslet.2015.08.014subject
Has Abstractpub_date
2015-09-14 00:00:00pages
2561-9issue
19 Pt Aeissn
0014-5793issn
1873-3468pii
S0014-5793(15)00713-9journal_volume
589pub_type
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