Alterovitz, Wei-LunFaraggi, EshelOldfield, Christopher J.Meng, JingweiXue, BinHuang, FeiRomero, PedroKloczkowski, AndrzejUversky, Vladimir N.Dunker, A. Keith2022-05-102022-05-102019-11-02Alterovitz, W.-L., Faraggi, E., Oldfield, C. J., Meng, J., Xue, B., Huang, F., Romero, P., Kloczkowski, A., Uversky, V. N., & Dunker, A. K. (2019). Many-to-one binding by intrinsically disordered protein regions. In Biocomputing 2020 (pp. 159–170). WORLD SCIENTIFIC. https://doi.org/10.1142/9789811215636_0015https://hdl.handle.net/1805/28900Disordered binding regions (DBRs), which are embedded within intrinsically disordered proteins or regions (IDPs or IDRs), enable IDPs or IDRs to mediate multiple protein-protein interactions. DBR-protein complexes were collected from the Protein Data Bank for which two or more DBRs having different amino acid sequences bind to the same (100% sequence identical) globular protein partner, a type of interaction herein called many-to-one binding. Two distinct binding profiles were identified: independent and overlapping. For the overlapping binding profiles, the distinct DBRs interact by means of almost identical binding sites (herein called “similar”), or the binding sites contain both common and divergent interaction residues (herein called “intersecting”). Further analysis of the sequence and structural differences among these three groups indicate how IDP flexibility allows different segments to adjust to similar, intersecting, and independent binding pockets.enAttribution-NonCommercial 4.0 Internationalbinding sitedisordered binding fragmentlinear motifmolecular recognition featureArticle