Heat Shock Protein 40: Structural Studies and Their Functional Implications

Author(s): Jingzhi Li, Xinguo Qian, Bingdong Sha

Journal Name: Protein & Peptide Letters

Volume 16 , Issue 6 , 2009

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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.

Keywords: Molecular chaperone, Hsp40, Hsp70, J-domain, peptide-binding fragment, protein structure, Sis1, Ydj1

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Article Details

Year: 2009
Published on: 01 March, 2012
Page: [606 - 612]
Pages: 7
DOI: 10.2174/092986609788490159
Price: $65

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