Expanding the Paradigm: Intrinsically Disordered Proteins and Allosteric Regulation

J Mol Biol. 2018 Aug 3;430(16):2309-2320. doi: 10.1016/j.jmb.2018.04.003. Epub 2018 Apr 7.

Abstract

Allosteric regulatory processes are implicated at all levels of biological function. Recent advances in our understanding of the diverse and functionally significant class of intrinsically disordered proteins have identified a multitude of ways in which disordered proteins function within the confines of the allosteric paradigm. Allostery within or mediated by intrinsically disordered proteins ensures robust and efficient signal integration through mechanisms that would be extremely unfavorable or even impossible for globular protein interaction partners. Here, we highlight recent examples that indicate the breadth of biological outcomes that can be achieved through allosteric regulation by intrinsically disordered proteins. Ongoing and future work in this rapidly evolving area of research will expand our appreciation of the central role of intrinsically disordered proteins in ensuring the fidelity and efficiency of cellular regulation.

Keywords: allostery; post-translational modification; protein disorder; protein–protein interaction.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Allosteric Regulation
  • Binding Sites
  • Gene Expression Regulation
  • Humans
  • Intrinsically Disordered Proteins / chemistry*
  • Intrinsically Disordered Proteins / metabolism*
  • Models, Molecular
  • Protein Conformation
  • Protein Folding
  • Thermodynamics

Substances

  • Intrinsically Disordered Proteins