Structural insights into the redox-regulated dynamic conformations of human protein disulfide isomerase.

@article{Wang2013StructuralII,
  title={Structural insights into the redox-regulated dynamic conformations of human protein disulfide isomerase.},
  author={Chao Wang and Wei Li and Jinqi Ren and Jingqi Fang and Huimin Ke and Weimin Gong and Wei Feng and Chih-chen Wang},
  journal={Antioxidants & redox signaling},
  year={2013},
  volume={19 1},
  pages={36-45}
}
AIM Human protein disulfide isomerase (hPDI) is a key enzyme and a redox-regulated chaperone responsible for oxidative protein folding in the endoplasmic reticulum. This work aims to reveal the molecular mechanism underlying the redox-regulated functions of hPDI by determining the crystal structures of hPDI in different redox states. RESULTS The structures of hPDI (abb'xa') in both the reduced and oxidized states showed that the four thioredoxin domains of a, b, b', and a' are arranged as a… CONTINUE READING