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 res idue of 3-hydroxyproline was identified, but for collagen X this was locate d near the N-terminal end of the helix. Lysine residues in collagen X are e xtensively hydroxylated/glycosylated: at least 11 sites were localized and shown to be fully glycosylated, exclusively as glucosyl-galactosyl derivati ves. The lysine-derived crosslinks, dihydroxylysinonorleucine and hydroxyly sinonorleucine, were shown to be present in a 3:2 molar ratio primarily wit hin the C-terminal portion of the helix. (C) 1999 Elsevier Science B.V./Int ernational Society of Matrix Biology. All rights reserved.