A substrate preference for the rough endoplasmic reticulum resident protein FKBP22 during collagen biosynthesis.

@article{Ishikawa2014ASP,
  title={A substrate preference for the rough endoplasmic reticulum resident protein FKBP22 during collagen biosynthesis.},
  author={Yoshihiro Ishikawa and Hans Peter B{\"a}chinger},
  journal={The Journal of biological chemistry},
  year={2014},
  volume={289 26},
  pages={18189-201}
}
The biosynthesis of collagens occurs in the rough endoplasmic reticulum and requires a large numbers of molecular chaperones, foldases, and post-translational modification enzymes. Collagens contain a large number of proline residues that are post-translationally modified to 3-hydroxyproline or 4-hydroxyproline, and the rate-limiting step in formation of the triple helix is the cis-trans isomerization of peptidyl-proline bonds. This step is catalyzed by peptidyl-prolyl cis-trans isomerases… CONTINUE READING