Literature DB >> 26851279

Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications.

Alaji Bah1, Julie D Forman-Kay2.   

Abstract

Post-translational modifications (PTMs) produce significant changes in the structural properties of intrinsically disordered proteins (IDPs) by affecting their energy landscapes. PTMs can induce a range of effects, from local stabilization or destabilization of transient secondary structure to global disorder-to-order transitions, potentially driving complete state changes between intrinsically disordered and folded states or dispersed monomeric and phase-separated states. Here, we discuss diverse biological processes that are dependent on PTM regulation of IDPs. We also present recent tools for generating homogenously modified IDPs for studies of PTM-mediated IDP regulatory mechanisms.
© 2016 by The American Society for Biochemistry and Molecular Biology, Inc.

Entities:  

Keywords:  intrinsically disordered protein; post-translational modification (PTM); protein conformation; protein-DNA interaction; protein-protein interaction; regulation

Mesh：

Substances：

Year:  2016        PMID： 26851279      PMCID： PMC4807257          DOI： 10.1074/jbc.R115.695056

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


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