| created | [InstanceEdit:8944228] Jupe, Steve, 2016-11-03 |
| dbId | 8944213 |
| displayName | The C-terminal propeptide is essential for the association o... |
| literatureReference |
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| modified | [InstanceEdit:8944316] Jupe, Steve, 2016-11-03 |
| schemaClass | Summation |
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The C-terminal propeptide is essential 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). |
| (summation) |
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