On the specificity of protein–protein interactions in the context of disorder
| Autor: | Birthe B. Kragelund, Kaare Teilum, Johan G. Olsen |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
Protein Folding
Protein Conformation BINDING-AFFINITY Globular protein multispecificity Biophysics specificity Context (language use) protein–protein interactions Computational biology Intrinsically disordered proteins Biochemistry Interactome Molecular Bases of Health & Disease SHORT LINEAR MOTIF Protein–protein interaction 03 medical and health sciences Structural Biology PIP BOX Animals Humans Protein Interaction Domains and Motifs PCNA-BINDING Review Articles Molecular Biology 030304 developmental biology chemistry.chemical_classification P53 0303 health sciences Molecular Interactions Chemistry 030302 biochemistry & molecular biology TRANSACTIVATION DOMAIN INTERACTION NATIVELY UNFOLDED PROTEINS Cell Biology multivalency PROTEIN-PROTEIN INTERACTION Intrinsically Disordered Proteins Structural biology Cell Cycle Growth & Proliferation INTRINSIC DISORDER LIQUID-PHASE-SEPARATION Protein Binding |
| Zdroj: | Teilum, K, Olsen, J G & Kragelund, B B 2021, ' On the specificity of protein-protein interactions in the context of disorder ', Biochemical Journal, vol. 478, no. 11, pp. 2035-2050 . https://doi.org/10.1042/BCJ20200828 Biochemical Journal |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bcj20200828 |
| Popis: | With the increased focus on intrinsically disordered proteins (IDPs) and their large interactomes, the question about their specificity — or more so on their multispecificity — arise. Here we recapitulate how specificity and multispecificity are quantified and address through examples if IDPs in this respect differ from globular proteins. The conclusion is that quantitatively, globular proteins and IDPs are similar when it comes to specificity. However, compared with globular proteins, IDPs have larger interactome sizes, a phenomenon that is further enabled by their flexibility, repetitive binding motifs and propensity to adapt to different binding partners. For IDPs, this adaptability, interactome size and a higher degree of multivalency opens for new interaction mechanisms such as facilitated exchange through trimer formation and ultra-sensitivity via threshold effects and ensemble redistribution. IDPs and their interactions, thus, do not compromise the definition of specificity. Instead, it is the sheer size of their interactomes that complicates its calculation. More importantly, it is this size that challenges how we conceptually envision, interpret and speak about their specificity. |
| Databáze: | OpenAIRE |
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