Structure and in Vivo Function of Hsp90

Curr Opin Struct Biol. 2000 Feb;10(1):46-51. doi: 10.1016/s0959-440x(99)00047-0.


Until recently, Hsp90 was one of the least well understood of the molecular chaperones, but considerable progress is now being made in unravelling its biochemistry. Hsp90 has now been shown to possess an inherent ATPase that is essential for the activation of authentic 'client' proteins in vivo and in vitro. The molecular detail of Hsp90's interactions with co-chaperones is also becoming clearer and the identification of key roles in assembling regulatory and signalling pathways has made it a target for anticancer drug development. Despite this, a clear understanding of how Hsp90 contributes to the folding and/or activation of its client proteins remains some way off.

Publication types

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

MeSH terms

  • Adenosine Triphosphate / physiology
  • Allosteric Regulation
  • Animals
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / physiology
  • Benzoquinones
  • HSP90 Heat-Shock Proteins / antagonists & inhibitors
  • HSP90 Heat-Shock Proteins / chemistry
  • HSP90 Heat-Shock Proteins / physiology*
  • Humans
  • Lactams, Macrocyclic
  • Macromolecular Substances
  • Models, Biological
  • Models, Molecular
  • Protein Binding
  • Quinones / pharmacology
  • Rifabutin / analogs & derivatives
  • Signal Transduction / physiology
  • Structure-Activity Relationship


  • Bacterial Proteins
  • Benzoquinones
  • HSP90 Heat-Shock Proteins
  • Lactams, Macrocyclic
  • Macromolecular Substances
  • Quinones
  • Rifabutin
  • herbimycin
  • Adenosine Triphosphate
  • geldanamycin