Oxidative protein folding in the mammalian endoplasmic reticulum
| Autor: | Catherine E. Jessop, Rachel H. Watkins, Neil J. Bulleid, Seema Chakravarthi |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
chemistry.chemical_classification
Protein Folding Binding Sites Endoplasmic reticulum Protein Disulfide-Isomerases STIM1 Plasma protein binding Biology Endoplasmic Reticulum Biochemistry Oxygen Secretory protein chemistry Oxidoreductase Animals Humans Protein folding Disulfides Binding site Protein disulfide-isomerase Oxidation-Reduction Protein Binding |
| Zdroj: | Biochemical Society transactions. 32(Pt 5) |
| ISSN: | 0300-5127 |
| Popis: | Native disulphide bonds are essential for the structure and function of many membrane and secretory proteins. Disulphide bonds are formed, reduced and isomerized in the endoplasmic reticulum of mammalian cells by a family of oxidoreductases, which includes protein disulphide isomerase (PDI), ERp57, ERp72, P5 and PDIR. This review will discuss how these enzymes are maintained in either an oxidized redox state that allows them to form disulphide bonds in substrate proteins or a reduced form that allows them to perform isomerization and reduction reactions, how these opposing pathways may co-exist within the same compartment and why so many oxidoreductases exist when PDI alone can perform all three of these functions. |
| Databáze: | OpenAIRE |
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