TY - JOUR T1 - Prediction of Protein Binding Regions in Disordered Proteins A1 - Mészáros, Bálint A1 - Simon, István A1 - Dosztányi, Zsuzsanna Y1 - 2009/05/01 N2 - Author Summary Intrinsically unstructured/disordered proteins (IUPs/IDPs) do not adopt a stable structure in isolation but exist as a highly flexible ensemble of conformations. Despite the lack of a well-defined structure these proteins carry out important functions. Many IUPs/IDPs function via binding specifically to other macromolecules that involves a disorder-to-order transition. The molecular recognition functions of IUPs/IDPs include regulatory and signaling interactions where binding to multiple partners and high-specificity/low-affinity interactions play a crucial role. Due to their specific functional and structural properties, these binding regions have distinct properties compared to both globular proteins and disordered regions in general. Here, we present a general method to identify disordered binding regions from the amino acid sequence. Our method targets the essential feature of these regions: they behave in a characteristically different manner in isolation than bound to their partner protein. This prediction method allows us to compare the binding properties of short and long binding sites. The evolutionary relationship between the amount of disordered binding regions and general disordered regions in various organisms was also analyzed. Our results suggest that disordered binding regions can be recognized even without taking into account their adopted secondary structure or their specific binding partner. JF - PLOS Computational Biology JA - PLOS Computational Biology VL - 5 IS - 5 UR - https://doi.org/10.1371/journal.pcbi.1000376 SP - e1000376 EP - PB - Public Library of Science M3 - doi:10.1371/journal.pcbi.1000376 ER -