Association of procollagen type VI

Stable Identifier
Reaction [binding]
Homo sapiens
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
The C-terminal propeptide region is required for the association of 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, Bornstein, P, Click, EM, Harper, E

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

Timpl, R, Brückner, P, Engel, J, Bächinger, HP

Eur J Biochem 1978
Orthologous Events
Cite Us!