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Heat shock protein 40: structural studies and their functional implications Li J; Qian X; Sha BProtein Pept Lett 2009[]; 16 (6): 606-12The 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.|Crystallography, X-Ray[MESH]|HSP40 Heat-Shock Proteins/*chemistry/genetics/*physiology[MESH]|HSP70 Heat-Shock Proteins/chemistry/genetics/physiology[MESH]|Humans[MESH]|Nuclear Magnetic Resonance, Biomolecular[MESH]|Protein Folding[MESH]|Protein Structure, Tertiary[MESH] |
