Protein binding and disruption by Clp/Hsp100 chaperones

Structure. 2004 Feb;12(2):175-83. doi: 10.1016/j.str.2004.01.021.


Clp/Hsp100 chaperones work with other cellular chaperones and proteases to control the quality and amounts of many intracellular proteins. They employ an ATP-dependent protein unfoldase activity to solubilize protein aggregates or to target specific classes of proteins for degradation. The structural complexity of Clp/Hsp100 proteins combined with the complexity of the interactions with their macromolecular substrates presents a considerable challenge to understanding the mechanisms by which they recognize and unfold substrates and deliver them to downstream enzymes. Fortunately, high-resolution structural data is now available for several of the chaperones and their functional partners, which together with mutational data on the chaperones and their substrates has provided a glimmer of light at the end of the Clp/Hsp100 tunnel.

Publication types

  • Review

MeSH terms

  • Endopeptidase Clp
  • Heat-Shock Proteins / chemistry*
  • Molecular Chaperones / chemistry*
  • Protein Binding
  • Protein Folding
  • Protein Structure, Tertiary / physiology
  • Protein Subunits / chemistry*
  • Protozoan Proteins / chemistry*


  • Heat-Shock Proteins
  • Molecular Chaperones
  • Protein Subunits
  • Protozoan Proteins
  • Endopeptidase Clp
  • ClpB protein, Leishmania