Advantages of proteins being disordered |
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| Authors: | Zhirong Liu Yongqi Huang |
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| Institution: | 1. College of Chemistry and Molecular Engineering, Peking University, , Beijing, 100871 China;2. Beijing National Laboratory for Molecular Sciences (BNLMS), Peking University, , Beijing, 100871 China;3. State Key Laboratory for Structural Chemistry of Unstable and Stable Species, Peking University, , Beijing, 100871 China;4. Center for Quantitative Biology, Peking University, , Beijing, 100871 China;5. Department of Structural Biology, St. Jude Children's Research Hospital, , Memphis, Tennessee, 38105 |
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| 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. |
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| Keywords: | intrinsically disordered proteins protein function flexibility protein‐protein interaction molecular recognition protein design drug design |
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