No abstract

No abstract

Background: Human protein-disulfide isomerase (hPDI) is a key enzyme and chaperone for protein folding. Results: Oxidation of domain aЈ releases the compact conformation of hPDI and exposes the buried substrate-binding sites facilitating its high chaperone activity. Conclusion: Oxidation of hPDI activates its chaperone activity. Significance: This study provides the first structural evidence of and mechanistic insights into the redox-regulated chaperone activity of hPDI.