Influence of core protein sequence on glycosaminoglycan assembly

JD Esko, L Zhang - Current opinion in structural biology, 1996 - Elsevier
Current opinion in structural biology, 1996Elsevier
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.
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.
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