To be disordered or not to be disordered: is that still a question for proteins in the cell?

TitleTo be disordered or not to be disordered: is that still a question for proteins in the cell?
Publication TypeJournal Article
Year of Publication2017
AuthorsPauwels, K., P. Lebrun, and P. Tompa
JournalCell Mol Life Sci
Volume74
Issue17
Pagination3185-3204
Date Published2017 09
ISSN1420-9071
Keywordsalpha-Synuclein, Evolution, Molecular, Humans, Intrinsically Disordered Proteins, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Tertiary, Proteome
Abstract

There is ample evidence that many proteins or regions of proteins lack a well-defined folded structure under native-like conditions. These are called intrinsically disordered proteins (IDPs) or intrinsically disordered regions (IDRs). Whether this intrinsic disorder is also their main structural characteristic in living cells has been a matter of intense debate. The structural analysis of IDPs became an important challenge also because of their involvement in a plethora of human diseases, which made IDPs attractive targets for therapeutic development. Therefore, biophysical approaches are increasingly being employed to probe the structural and dynamical state of proteins, not only in isolation in a test tube, but also in a complex biological environment and even within intact cells. Here, we survey direct and indirect evidence that structural disorder is in fact the physiological state of many proteins in the proteome. The paradigmatic case of α-synuclein is used to illustrate the controversial nature of this topic.

DOI10.1007/s00018-017-2561-6
Alternate JournalCell. Mol. Life Sci.
PubMed ID28612216
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