Protein disulfide isomerases exploit synergy between catalytic and specific binding domains

Lignende værker

• The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins.
  af: Klappa, P, et al.
  Udgivet: (1998)
• Specificity in substrate binding by protein folding catalysts: tyrosine and tryptophan residues are the recognition motifs for the binding of peptides to the pancreas-specific protein disulfide isomerase PDIp.
  af: Ruddock, L. W., et al.
  Udgivet: (2000)
• Protein disulfide isomerase isomerizes non-native disulfide bonds in human proinsulin independent of its peptide-binding activity
  af: Winter, Jeannette, et al.
  Udgivet: (2011)
• Structure of the third catalytic domain of the protein disulfide isomerase ERp46
  af: Gulerez, Irina E., et al.
  Udgivet: (2012)
• The ligand-binding b′ domain of human protein disulphide-isomerase mediates homodimerization
  af: Wallis, Anne Katrine, et al.
  Udgivet: (2009)