Influence of core protein sequence on glycosaminoglycan assembly
Recent studies have revealed a correlation between amino acid sequences around
glycosylation sites in proteoglycans and the ability of cells to initiate and process
glycosaminoglycan chains. Initiation depends on Ser—Gly/Ala dipeptides that have one or
more acidic amino acids in close proximity. The formation of heparan sulfate chains
depends on a nearby cluster of acidic residues, hydrophobic amino acids, and the close
spacing of glycosylation sites.
glycosylation sites in proteoglycans and the ability of cells to initiate and process
glycosaminoglycan chains. Initiation depends on Ser—Gly/Ala dipeptides that have one or
more acidic amino acids in close proximity. The formation of heparan sulfate chains
depends on a nearby cluster of acidic residues, hydrophobic amino acids, and the close
spacing of glycosylation sites.
Recent studies have revealed a correlation between amino acid sequences around glycosylation sites in proteoglycans and the ability of cells to initiate and process glycosaminoglycan chains. Initiation depends on Ser—Gly/Ala dipeptides that have one or more acidic amino acids in close proximity. The formation of heparan sulfate chains depends on a nearby cluster of acidic residues, hydrophobic amino acids, and the close spacing of glycosylation sites.
Elsevier