Abstract:Protein disulfide isomerase (PDI) catalyzes thiol oxidation, reduction and isomerization of disulphide bond of cell surface and secreted proteins. Yeast PDI1 consists of two catalytic domains (a and a') which are separated by two non-catalytic domains (b and b'), and a x region linked the b' and a domains. The b' domain is important for the non-covalent binding of partially folded protein. To understand the contribution of b' domain and x-linker of yeast PDI1 we have deleted the b'x and investigated its functi… Show more
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