Intrinsically unstructured proteins and their functions

Nat Rev Mol Cell Biol. 2005 Mar;6(3):197-208. doi: 10.1038/nrm1589.

Abstract

Many gene sequences in eukaryotic genomes encode entire proteins or large segments of proteins that lack a well-structured three-dimensional fold. Disordered regions can be highly conserved between species in both composition and sequence and, contrary to the traditional view that protein function equates with a stable three-dimensional structure, disordered regions are often functional, in ways that we are only beginning to discover. Many disordered segments fold on binding to their biological targets (coupled folding and binding), whereas others constitute flexible linkers that have a role in the assembly of macromolecular arrays.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • CREB-Binding Protein
  • Humans
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / genetics
  • Nuclear Proteins / physiology
  • Nucleic Acids / metabolism
  • Protein Binding
  • Protein Processing, Post-Translational
  • Protein Structure, Tertiary*
  • Proteins / chemistry*
  • Proteins / physiology*
  • Trans-Activators / chemistry
  • Trans-Activators / genetics
  • Trans-Activators / physiology
  • Tumor Suppressor Protein p53 / chemistry
  • Tumor Suppressor Protein p53 / physiology

Substances

  • Nuclear Proteins
  • Nucleic Acids
  • Proteins
  • Trans-Activators
  • Tumor Suppressor Protein p53
  • CREB-Binding Protein
  • CREBBP protein, human