Reactome | Association of procollagen type XIV

Association of procollagen type XIV

Stable Identifier

R-HSA-8944236

Type

Reaction [binding]

Species

Homo sapiens

Compartment

endoplasmic reticulum lumen

ReviewStatus

5/5

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The C-terminal region of the propeptide is required for association of the three alpha chains into a trimeric non-helical procollagen. Alignment determines the composition of the trimer, brings the individual chains into the correct register and initiates formation of the triple helix at the C-terminus, which then proceeds to the N-terminus in a zipper-like fashion (Engel & Prockop 1991). Most early refolding studies were performed with collagen type III which contains a disulfide linkage at the C-terminus of its triple helix (Bächinger et al. 1978, Bruckner et al. 1978) that acts as a permanent linker even after removal of the non-collagenous domains.

Mutations within the C-propeptides further suggest that they are crucial for the correct interaction of the three polypeptide chains and for subsequent correct folding (refs. in Boudko et al. 2011).

Literature References

PubMed ID	Title	Journal	Year
171650	Interchain disulfide bonds in procollagen are located in a large nontriple-helical COOH-terminal domain Byers, PH, Click, EM, Harper, E, Bornstein, P	Proc Natl Acad Sci U S A	1975
710450	The role of cis-trans isomerization of peptide bonds in the coil leads to and comes from triple helix conversion of collagen Bächinger, HP, Brückner, P, Timpl, R, Engel, J	Eur J Biochem	1978