Intrinsically disordered proteins: emerging interaction specialists

Curr Opin Struct Biol. 2015 Dec;35:49-59. doi: 10.1016/j.sbi.2015.08.009. Epub 2015 Sep 21.

Abstract

Intrinsically disordered proteins or regions of proteins (IDPs/IDRs) most often function through protein-protein interactions, when they permanently or transiently bind partner molecules with diverse functional consequences. There is a rapid advance in our understanding of the ensuing functional modes, obtained from describing atomic details of individual complexes, proteome-wide studies of interactomes and characterizing loosely assembled hydrogels and tightly packed amyloids. Here we briefly survey the most important recent methodological developments and structural-functional observations, with the aim of increasing the general appreciation of IDPs/IDRs as 'interaction specialists'.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Humans
  • Intrinsically Disordered Proteins / chemistry
  • Intrinsically Disordered Proteins / metabolism*
  • Molecular Mimicry
  • Molecular Sequence Data
  • Protein Interaction Mapping
  • Protein Processing, Post-Translational

Substances

  • Intrinsically Disordered Proteins