Structure of the glycosaminoglycan domain in the type IX collagen-proteoglycan.

• DOI: 10.1073/pnas.84.12.4044
• Publication Date: 2006-05-31T10:19:58Z
• Authors: D McCormick; M van der Rest; J Goodship; G Lozano; Y Ninomiya; B R Olsen
• Keywords: Dermatan sulfate

Type IX collagen represents 5-20% of the total in hyaline cartilage. The molecules this are composed three genetically distinct polypeptide subunits. One these subunits, alpha 2(IX), contains covalently bound glycosaminoglycan (chondroitin sulfate or dermatan sulfate). We report here on structure attachment site type collagen-proteoglycan. show, by a combination cDNA and peptide sequencing, that region sequence Gly-Ser-Ala-Asp, located within noncollagenous domain NC3 2(IX) chain. By comparing exons encoding 1(IX) genes, we find exon coding for gene is 48 base pairs long, whereas homologous 33 pairs. is, therefore, five amino acid residues longer than 1(IX). extra Val-Glu-Gly-Ser-Ala, provides simple explanation kink observed at when examined electron microscopy. inserted block also chains with serine residue, not present serves as side Our data show surrounds glycosylated residue collagen-proteoglycan differs from sequences core proteins. provide strong evidence glycosylation chance domain, but specific post-translational modification unusual molecule.