Intrinsically disordered proteins and intrinsically disordered protein regions

Christopher J. Oldfield, A. Keith Dunker

Research output: Contribution to journalArticle

356 Scopus citations

Abstract

Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet they exhibit biological activities. Their mobile flexibility and structural instability are encoded by their amino acid sequences. They recognize proteins, nucleic acids, and other types of partners; they accelerate interactions and chemical reactions between bound partners; and they help accommodate posttranslational modifications, alternative splicing, protein fusions, and insertions or deletions. Overall, IDP-Associated biological activities complement those of structured proteins. Recently, there has been an explosion of studies on IDP regions and their functions, yet the discovery and investigation of these proteins have a long, mostly ignored history. Along with recent discoveries, we present several early examples and the mechanisms by which IDPs contribute to function, which we hope will encourage comprehensive discussion of IDPs and IDP regions in biochemistry textbooks. Finally, we propose future directions for IDP research.

Original languageEnglish (US)
Pages (from-to)553-584
Number of pages32
JournalAnnual Review of Biochemistry
Volume83
DOIs
StatePublished - Jun 2014

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Keywords

  • chameleon
  • flexible
  • inherently
  • malleable
  • natively
  • rheomorphic
  • unfolded
  • unstructured

ASJC Scopus subject areas

  • Biochemistry
  • Medicine(all)

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