P4HB binds Collagen chains

Stable Identifier
R-HSA-2002460
Type
Reaction [binding]
Species
Homo sapiens
Compartment
endoplasmic reticulum lumen
Synonyms
PDI is a chaperone for collagen peptides
ReviewStatus
5/5
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P4HB binds Collagen chains
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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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Orthologous Events
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Authored
Jupe, S  (2010-07-20)
Reviewed
Canty-Laird, EG  (2012-05-24)
Created
Jupe, S  (2011-11-21)
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