Heat shock protein 40: structural studies and their functional implications.
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.
Li
Jingzhi
J
Department of Cell Biology, University of Alabama at Birmingham, AL 35294, USA.
Qian
Xinguo
X
Sha
Bingdong
B
D018360:Crystallography, X-Ray; D050956:HSP40 Heat-Shock Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D017510:Protein Folding; D017434:Protein Structure, Tertiary
D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins