Heat shock protein 40: Structural studies and their functional implications

Academic Article

Abstract

  • The mechanism by which Hsp40 and other molecular chaperones recognize and interact with non-native polypeptides is a fundamental question, as is how Hsp40 co-operates with Hsp70 to facilitate protein folding. Years of structural studies of Hsp40 from yeast and other species, conducted using X-ray protein crystallography, NMR and small-angle X-ray scattering, have shed light on the mechanisms how Hsp40 functions as a molecular chaperone and how Hsp40- Hsp70 pair promotes protein folding, protein transport and degradation. This review provides a discussion of recent structural studies of Hsp40s and their functional implications. © 2009 Bentham Science Publishers Ltd.
  • Published In

    Digital Object Identifier (doi)

    Author List

  • Li J; Qian X; Sha B
  • Start Page

  • 606
  • End Page

  • 612
  • Volume

  • 16
  • Issue

  • 6