期刊
PROTEIN SCIENCE
卷 24, 期 6, 页码 909-922出版社
WILEY
DOI: 10.1002/pro.2674
关键词
disordered proteins; disorder-to-order transitions; macromolecular protein assemblies; IDRs in protein complexes
资金
- Medical Research Council [MC_U105185859]
- Lister Institute Research Prize
- Marie Curie IOF
- MRC [MC_U105185859] Funding Source: UKRI
- Medical Research Council [MC_U105185859, 1416270, 1274107] Funding Source: researchfish
The traditional structure to function paradigm conceives of a protein's function as emerging from its structure. In recent years, it has been established that unstructured, intrinsically disordered regions (IDRs) in proteins are equally crucial elements for protein function, regulation and homeostasis. In this review, we provide a brief overview of how IDRs can perform similar functions to structured proteins, focusing especially on the formation of protein complexes and assemblies and the mediation of regulated conformational changes. In addition to highlighting instances of such functional equivalence, we explain how differences in the biological and physicochemical properties of IDRs allow them to expand the functional and regulatory repertoire of proteins. We also discuss studies that provide insights into how mutations within functional regions of IDRs can lead to human diseases.
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