Redox-Dependent Chaperoning Following PDI Footsteps
Olivier Serve, Yukiko Kamiya and Koichi Kato
National Institutes of Natural Sciences, Japan, and others
Series: Protein Biochemistry, Synthesis, Structure and Cellular Functions
BISAC: SCI007000
Details
Protein disulfide isomerase (PDI) is a protein-folding assistant and a molecular chaperone found in the endoplasmic reticulum. This enzyme catalyzes the formation and the isomerization of disulfide bonds. The binding and release of substrate from molecular chaperones are usually triggered by cycles of ATP hydrolysis. It has been proposed that the substrate binding / release cycle of PDI could be correlated with the redox states of its active sites. This book examines the differences between the domains that compose PDI in regards to their functions and the consequences of the conformational alteration they experience upon redox condition changes. (Imprint: Nova)
ABSTRACT
INTRODUCTION
MODULARITY OF PDI
FUNCTIONAL NON-EQUIVALENCE IF HOMOLOGOUS DOMAINS
REDOX DEPENDENCE OF THE BINDING PROPERTIES
CONFORMATIONAL REARRANGEMENT
CONCLUSION
ACKNOWLEDGEMENTS
REFERENCES
INDEX
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