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Trends Biochem Sci. 1999 Apr;24(4):136-41.

Hsp90 & Co. - a holding for folding.

Author information

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

Abstract

Hsp90 is an abundant molecular chaperone that is involved in the folding of a defined set of signalling molecules including steroid-hormone receptors and kinases. Recent in vitro experiments suggest that Hsp90 contains two different binding sites for non-native proteins, which allow it to combine the properties of a promiscuous chaperone with those of a dedicated folding-helper protein. Significant progress has been made in analysing co-chaperones, which form defined, substrate-dependent complexes with Hsp90 in vivo. Structural studies have identified the ATP-binding site in the N-terminal domain of Hsp90, which can be blocked by high-affinity inhibitors. Although a detailed understanding of the mechanism of Hsp90 action is still lacking, recent advances suggest that the protein is the centre of a dynamic, multifunctional and multicomponent chaperone machinery that extends the limits of protein folding in the cell.

PMID:
10322418
[PubMed - indexed for MEDLINE]
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