Dataset Information
Analysis of proline and lysine post-translational modifications of collagen from prolyl 3-hydroxylase 3 and lysyl hydroxylase 1 null mice
Ontology highlight
ABSTRACT:
ORGANISM(S): Mus Musculus (mouse)
SUBMITTER: Yoshihiro Ishikawa
PROVIDER: PXD019748 | JPOST Repository | Fri Feb 19 00:00:00 GMT 2021
REPOSITORIES: jPOST
Publications
Type I and type V procollagen triple helix uses different subsets of the molecular ensemble for lysine posttranslational modifications in the rER.
The Journal of biological chemistry 20210101
Collagen is the most abundant protein in humans. It has a characteristic triple-helix structure and is heavily posttranslationally modified. The complex biosynthesis of collagen involves processing by many enzymes and chaperones in the rough endoplasmic reticulum. Lysyl hydroxylase 1 (LH1) is required to hydroxylate lysine for cross-linking and carbohydrate attachment within collagen triple helical sequences. Additionally, a recent study of prolyl 3-hydroxylase 3 (P3H3) demonstrated that this en ...[more]
