A structural overview of the PDI family of proteins.
Protein disulfide isomerases (PDIs) are enzymes that mediate oxidative protein folding in the endoplasmic reticulum. Understanding of PDIs has historically been hampered by lack of structural information. Over the last several years, partial and full-length PDI structures have been solved at an increasing rate. Analysis of the structures reveals common features shared by several of the best known PDI family members, and also unique features related to substrate and partner binding sites. These exciting breakthroughs provide a deeper understanding of the mechanisms of oxidative protein folding in cells.
Kozlov
Guennadi
G
Department of Biochemistry, McGill University, Montréal, Québec, Canada.
Määttänen
Pekka
P
Thomas
David Y
DY
Gehring
Kalle
K
D001665:Binding Sites; D020134:Catalytic Domain; D004721:Endoplasmic Reticulum / Q000201:enzymology; D006801:Humans; D008958:Models, Molecular; D010088:Oxidoreductases / Q000502:physiology; D011487:Protein Conformation; D019704:Protein Disulfide-Isomerases / Q000737:chemistry / Q000378:metabolism*; D017510:Protein Folding; D011506:Proteins / Q000502:physiology*; D013379:Substrate Specificity; D013879:Thioredoxins / Q000737:chemistry / Q000378:metabolism
D011506:Proteins; D013879:Thioredoxins; D010088:Oxidoreductases; C526506:PDIA5 protein, human; D019704:Protein Disulfide-Isomerases