Intrinsic Disorder, Protein–Protein Interactions, and Disease

Document Type

Book Chapter

Publication Date

2018

Keywords

Intrinsically disordered protein, Intrinsically disordered protein region, Protein–protein interaction, Proteinaceous membrane-less organelle, Conformational disease

Digital Object Identifier (DOI)

https://doi.org/10.1016/bs.apcsb.2017.06.005

Abstract

It is recognized now that biologically active proteins without stable tertiary structure (known as intrinsically disordered proteins, IDPs) and hybrid proteins containing ordered domains and intrinsically disordered protein regions (IDPRs) are important players found in any given proteome. These IDPs/IDPRs possess functions that complement functional repertoire of their ordered counterparts, being commonly related to recognition, as well as control and regulation of various signaling pathways. They are interaction masters, being able to utilize a wide spectrum of interaction mechanisms, ranging from induced folding to formation of fuzzy complexes where significant levels of disorder are preserved, to polyvalent stochastic interactions playing crucial roles in the liquid–liquid phase transitions leading to the formation of proteinaceous membrane-less organelles. IDPs/IDPRs are tightly controlled themselves via various means, including alternative splicing, precisely controlled expression and degradation, binding to specific partners, and posttranslational modifications. Distortions in the regulation and control of IDPs/IDPRs, as well as their aberrant interactivity are commonly associated with various human diseases. This review presents some aspects of the intrinsic disorder-based functionality and dysfunctionality, paying special attention to the normal and pathological protein–protein interactions.

Was this content written or created while at USF?

Yes

Citation / Publisher Attribution

Intrinsic Disorder, Protein–Protein Interactions, and Disease, in R. Donev (Ed.), Advances in Protein Chemistry and Structural Biology, v.110, Academic Press, p. 85-121

Share

COinS