Primary structure of the helical domain of porcine collagen X.
The entire primary structure of the collagen X helical region is presented, including identification of the extensive post-ribosomal modifications by amino acid sequencing and mass spectrometry. As in collagen I, a single residue of 3-hydroxyproline was identified, but for collagen X this was located near the N-terminal end of the helix. Lysine residues in collagen X are extensively hydroxylated/glycosylated: at least 11 sites were localized and shown to be fully glycosylated, exclusively as glucosyl-galactosyl derivatives. The lysine-derived crosslinks, dihydroxylysinonorleucine and hydroxylysinonorleucine, were shown to be present in a 3:2 molar ratio primarily within the C-terminal portion of the helix.
Bos
K J
KJ
The Rowett Research Institute, Skeletal Research Unit, Aberdeen, Scotland, UK.
Rucklidge
G J
GJ
Dunbar
B
B
Robins
S P
SP
D000595:Amino Acid Sequence; D000818:Animals; D003094:Collagen / Q000737:chemistry* / Q000378:metabolism; D006031:Glycosylation; D008239:Lysine; D008969:Molecular Sequence Data; D017421:Sequence Analysis; D013552:Swine
D003094:Collagen; D008239:Lysine