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

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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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