Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 291, Issue 13, Pages 6681-6688Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.R115.685859
Keywords
intrinsically disordered protein; multifunctional protein; post-translational modification (PTM); protein folding; protein-protein interaction; complexity; dynamical system; structural heterogeneity; intrinsically disordered proteins; posttranslational modification
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Funding
- Russian Science Foundation RSCF [14-24-00131]
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Biologically active but floppy proteins represent a new reality of modern protein science. These intrinsically disordered proteins (IDPs) and hybrid proteins containing ordered and intrinsically disordered protein regions (IDPRs) constitute a noticeable part of any given proteome. Functionally, they complement ordered proteins, and their conformational flexibility and structural plasticity allow them to perform impossible tricks and be engaged in biological activities that are inaccessible to well folded proteins with their unique structures. The major goals of this minireview are to show that, despite their simplified amino acid sequences, IDPs/IDPRs are complex entities often resembling chaotic systems, are structurally and functionally heterogeneous, and can be considered an important part of the structure-function continuum. Furthermore, IDPs/IDPRs are everywhere, and are ubiquitously engaged in various interactions characterized by a wide spectrum of binding scenarios and an even wider spectrum of structural and functional outputs.
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