Association of procollagen type XXI

Stable Identifier
R-HSA-8944246
Type
Reaction
Species
Homo sapiens
Compartment
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Summation

The C-terminal propeptide region is necessary to allow 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
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
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
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