P4HB binds Collagen chains

Stable Identifier
R-HSA-2002460
Type
Reaction [binding]
Species
Homo sapiens
Compartment
Synonyms
PDI is a chaperone for collagen peptides
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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).

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