|Title||How proteins form disulfide bonds.|
|Publication Type||Journal Article|
|Year of Publication||2011|
|Authors||Depuydt, M., J. Messens, and J-F. Collet|
|Journal||Antioxid Redox Signal|
|Date Published||2011 Jul 1|
|Type of Article||redox|
|Keywords||Animals, Bacterial Proteins, Disulfides, Endoplasmic Reticulum, Humans, Membrane Proteins, Protein Disulfide-Isomerases, Protein Folding|
The identification of protein disulfide isomerase, almost 50 years ago, opened the way to the study of oxidative protein folding. Oxidative protein folding refers to the composite process by which a protein recovers both its native structure and its native disulfide bonds. Pathways that form disulfide bonds have now been unraveled in the bacterial periplasm (disulfide bond protein A [DsbA], DsbB, DsbC, DsbG, and DsbD), the endoplasmic reticulum (protein disulfide isomerase and Ero1), and the mitochondrial intermembrane space (Mia40 and Erv1). This review summarizes the current knowledge on disulfide bond formation in both prokaryotes and eukaryotes and highlights the major problems that remain to be solved.
|Alternate Journal||Antioxid. Redox Signal.|
How proteins form disulfide bonds.