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.
Division of Cellular and Molecular Medicine, University of California, San Diego, La Jolla 92093-0687, USA. jesko@ucsd.edu
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D000595:Amino Acid Sequence; D000818:Animals; D006025:Glycosaminoglycans / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D015394:Molecular Structure; D017421:Sequence Analysis; D014758:Viral Core Proteins / Q000737:chemistry*
D006025:Glycosaminoglycans; D014758:Viral Core Proteins