Regulation and specificity of the human disulphide catalyst Ero1-La
The formation of disulphide bonds within many proteins, especially those that are secreted, is essential for their correct folding, stability and function. Disulphlde bonds are formed within the lumen of the Endoplasmic Reticulum (ER) in mammalian cells. Protein disulphide isomerase (PDI) oxidises c...
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University of Manchester
2008
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| Online Access: | http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.491846 |
| Summary: | The formation of disulphide bonds within many proteins, especially those that are secreted, is essential for their correct folding, stability and function. Disulphlde bonds are formed within the lumen of the Endoplasmic Reticulum (ER) in mammalian cells. Protein disulphide isomerase (PDI) oxidises cysteine residues in substrate proteins, resulting in the insertion of disulphide bonds into the substrate and the reduction of the oxidised PDI active-site. For PDI to act as an oxidase it needs to have its active-site in an oxidised state. The re-oxidation of PDI is thought to be carried out by the actions of endoplasmic reticulum oxidoreductin 1 (Erol). The aim of this project was to purify recombinant Human Erol-La;, determining its ability to oxidise PDI and to carry out a structure/function analysis to understand how Erol-La; is regulated. |
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