publication . Other literature type . Article . 2013

THE CXXXC MOTIF REVEALS DISULFIDE ISOMERASE ACTIVITY IN VITRO

Yoshihiro Ishikawa; Hans Peter Bächinger;
Open Access English
  • Published: 16 Sep 2013
  • Publisher: American Society for Biochemistry and Molecular Biology
Abstract
Abstract Collagen biosynthesis occurs in the rough endoplasmic reticulum, and many molecular chaperones and folding enzymes are involved in this process. The folding mechanism of type I procollagen has been well characterized, and protein disulfide isomerase (PDI) has been suggested as a key player in the formation of the correct disulfide bonds in the noncollagenous carboxyl-terminal and amino-terminal propeptides. Prolyl 3-hydroxylase 1 (P3H1) forms a hetero-trimeric complex with cartilage-associated protein and cyclophilin B (CypB). This complex is a multifunctional complex acting as a prolyl 3-hydroxylase, a peptidyl prolyl cis-trans isomerase, and a molecul...
Subjects
free text keywords: Glycobiology and Extracellular Matrices, Cell Biology, Biochemistry, Molecular Biology, Biology, Protein disulfide-isomerase, Protein precursor, Peptide, chemistry.chemical_classification, chemistry, Isomerase, Dioxygenase, Chaperone (protein), biology.protein, Enzyme, Endoplasmic reticulum
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