‘Something in the way she moves’: The functional significance of flexibility in the multiple roles of protein disulfide isomerase (PDI)

• Published in: Biochimica et biophysica acta Vol. 1865; no. 11; pp. 1383 - 1394
• Main Authors: Freedman, Robert B., Desmond, Jasmine L., Byrne, Lee J., Heal, Jack W., Howard, Mark J., Sanghera, Narinder, Walker, Kelly L., Wallis, A. Katrine, Wells, Stephen A., Williamson, Richard A., Römer, Rudolf A.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.11.2017; Elsevier Pub. Co
• Subjects: Animals; Biocatalysis; Conserved Sequence; Endoplasmic reticulum; Endoplasmic Reticulum - enzymology; Gene Expression; Humans; Molecular Chaperones - chemistry; Molecular Chaperones - genetics; Molecular Chaperones - metabolism; Molecular Dynamics Simulation; Oxidation-Reduction; Oxidative protein folding; Protein disulfide isomerase; Protein Disulfide-Isomerases - chemistry; Protein Disulfide-Isomerases - genetics; Protein Disulfide-Isomerases - metabolism; Protein Domains; Protein dynamics; Protein Folding; Protein Structure, Secondary; Saccharomyces cerevisiae - enzymology; Saccharomyces cerevisiae - genetics; Structural Homology, Protein; Protein disulfide isomerase; Protein dynamics; Oxidative protein folding; Endoplasmic reticulum

Protein disulfide isomerase (PDI) has diverse functions in the endoplasmic reticulum as catalyst of redox transfer, disulfide isomerization and oxidative protein folding, as molecular chaperone and in multi-subunit complexes. It interacts with an extraordinarily wide range of substrate and partner p...