Source:http://www.reactome.org/biopax/48887BiochemicalReaction642
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As the collagen peptide chain is translocated across the membrane of the endoplasmic reticulum, intrachain disulfide bonds are formed within the N- and C-propeptides. This allows the triple helical domain to form a nucleation point at its C-terminal end and ensures correct alignment of the chains (Engel & Prockop 1991). Protein disulfide isomerase (P4HB) catalyzes the formation of both intra- (Bulleid & Freedman 1988) and inter-chain disulfide bonds (Koivu & Myllylä 1987). In addition, PDI acts as a molecular chaperone, interacting with monomeric collagen propeptide chains to prevent premature assembly or aggregation (Wilson et al. 1998).,
Authored: Jupe, S, 2010-07-20,
Edited: Jupe, S, 2012-05-14,
Reviewed: Canty-Laird, EG, 2012-05-24
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http://identifiers.org/pubmed/1867713,
http://identifiers.org/pubmed/3173483,
http://identifiers.org/pubmed/3571251,
http://identifiers.org/pubmed/9545296,
http://identifiers.org/pubmed/9560306,
urn:biopax:UnificationXref:REACTOME DATABASE ID_2002460,
urn:biopax:UnificationXref:REACTOME_REACT_120881_1
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PDI is a chaperone for collagen peptides
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