title: Advantages of proteins being disordered.
abstract: The past decade has witnessed great advances in our understanding of protein structure-function relationships in terms of the ubiquitous existence of intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs). The structural disorder of IDPs/IDRs enables them to play essential functions that are complementary to those of ordered proteins. In addition, IDPs/IDRs are persistent in evolution. Therefore, they are expected to possess some advantages over ordered proteins. In this review, we summarize and survey nine possible advantages of IDPs/IDRs: economizing genome/protein resources, overcoming steric restrictions in binding, achieving high specificity with low affinity, increasing binding rate, facilitating posttranslational modifications, enabling flexible linkers, preventing aggregation, providing resistance to non-native conditions, and allowing compatibility with more available sequences. Some potential advantages of IDPs/IDRs are not well understood and require both experimental and theoretical approaches to decipher. The connection with protein design is also briefly discussed.
authors: College of Chemistry and Molecular Engineering, Peking University, Beijing, 100871, China; Beijing National Laboratory for Molecular Sciences (BNLMS), Peking University, Beijing, 100871, China; State Key Laboratory for Structural Chemistry of Unstable and Stable Species, Peking University, Beijing, 100871, China; Center for Quantitative Biology, Peking University, Beijing, 100871, China.
authors: Zhirong
authors: Z
authors: Liu
authors: Yongqi
authors: Y
authors: Huang
mesh_terms: D000818:Animals; D016678:Genome; D006801:Humans; D064267:Intrinsically Disordered Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D060066:Protein Interaction Maps; D011499:Protein Processing, Post-Translational
chemical_list: D064267:Intrinsically Disordered Proteins
keywords: drug design; flexibility; intrinsically disordered proteins; molecular recognition; protein design; protein function; protein-protein interaction