Coiled coils meet the chaperone world

Trends Biochem Sci. 2004 Sep;29(9):455-8. doi: 10.1016/j.tibs.2004.07.004.

Abstract

Coiled coils are versatile structural modules that engage in a variety of cellular activities. Recent studies illuminate their role as substrate-binding elements in the chaperone cofactor prefoldin and in the AAA+ ATPases involved in protein (un)folding processes. The use of coiled coils to mediate the binding of non-native proteins represents a novel strategy in chaperone design and a new function for coiled coils.

Publication types

  • Review

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Archaeal Proteins / chemistry
  • Archaeal Proteins / metabolism
  • Models, Molecular
  • Molecular Chaperones / chemistry
  • Molecular Chaperones / metabolism*
  • Protein Conformation
  • Protein Subunits / chemistry
  • Protein Subunits / metabolism
  • Substrate Specificity

Substances

  • Archaeal Proteins
  • Molecular Chaperones
  • Protein Subunits
  • prefoldin
  • Adenosine Triphosphatases