Protein disulphide isomerase: building bridges in protein folding.
Protein disulphide isomerase (PDI) has been known for many years to assist in the folding of proteins containing disulphide bonds, but the exact mechanism by which it achieves this is only now becoming clear. The active site of PDI closely resembles that of the redox protein thioredoxin, and cDNA cloning has revealed a superfamily of proteins with related active-site sequences, in organisms ranging from bacteria to higher animals and plants. Recent mutagenesis studies are now helping to unravel the catalytic mechanism of PDI, and work in yeast and other systems is clarifying the physiological roles of the multiple PDI-related proteins.
Freedman
R B
RB
Research School of Biosciences, Biological Laboratory, University of Kent, Canterbury, UK.
Hirst
T R
TR
Tuite
M F
MF
D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D007535:Isomerases / Q000737:chemistry / Q000502:physiology*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D019704:Protein Disulfide-Isomerases; D017510:Protein Folding; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013879:Thioredoxins / Q000737:chemistry
D013879:Thioredoxins; D007535:Isomerases; D019704:Protein Disulfide-Isomerases