Article
Mutations in domain a' of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease A.
Protein science : a publication of the Protein Society - 1 May 2003
Ruoppolo Margherita, Orrù Stefania, Talamo Fabio, Ljung Johanna, Pirneskoski Annamari, Kivirikko Kari I, Marino Gennaro, Koivunen Peppi
Abstract excerpt
Protein disulfide isomerase (PDI, EC 5.3.4.1), an enzyme and chaperone, catalyses disulfide bond formation and rearrangements in protein folding. It is also a subunit in two proteins, the enzyme collagen prolyl 4-hydroxylase and the microsomal triglyceride transfer protein. It consists of two catalytically active domains, a and a', and two inactive ones, b and b', all four domains having the thioredoxin fold....
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