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Hsp90 & Co. - a holding for folding.

J Buchner1

  • 1Institut für Organische Chemie & Biochemie, Technische Universität München, Lichtenbergstr. 4, 85747 München, Germany. johannes.buchner@ch.tum.de

Trends in Biochemical Sciences
|May 14, 1999
PubMed
Summary

Heat shock protein 90 (Hsp90) acts as a versatile molecular chaperone, aiding protein folding through a dynamic machinery. Its dual binding sites and co-chaperones highlight its complex cellular role.

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Area of Science:

  • Molecular biology
  • Protein folding
  • Cellular processes

Background:

  • Heat shock protein 90 (Hsp90) is a crucial molecular chaperone.
  • It facilitates the folding of key signaling molecules like receptors and kinases.
  • Hsp90 functions within a complex network of co-chaperones.

Purpose of the Study:

  • To explore the multifaceted nature of Hsp90's chaperone activity.
  • To understand the role of Hsp90's distinct binding sites.
  • To elucidate the mechanisms of Hsp90 in protein folding.

Main Methods:

  • In vitro experiments to analyze Hsp90 binding sites.
  • In vivo studies of Hsp90-co-chaperone complexes.
  • Structural studies identifying the ATP-binding site.

Main Results:

  • Hsp90 possesses two distinct binding sites for non-native proteins.
  • These sites enable Hsp90 to act as both a promiscuous and dedicated folding helper.
  • The ATP-binding site in the N-terminal domain is a target for inhibitors.

Conclusions:

  • Hsp90 operates as a central component of a dynamic, multi-component chaperone machinery.
  • This machinery expands the cell's capacity for protein folding.
  • Further understanding of Hsp90's mechanism is emerging from recent advances.

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