Heat Shock Protein 40: Structural Studies and Their Functional Implications
Jingzhi Li, Xinguo Qian and Bingdong Sha
Pages 606-612 (7)
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.
Molecular chaperone, Hsp40, Hsp70, J-domain, peptide-binding fragment, protein structure, Sis1, Ydj1
Department of Cell Biology, University of Alabama at Birmingham, Birmingham, AL 35294-0005, USA.