Esko J D, Zhang L
Division of Cellular and Molecular Medicine, University of California, San Diego, La Jolla 92093-0687, USA.
Curr Opin Struct Biol. 1996 Oct;6(5):663-70. doi: 10.1016/s0959-440x(96)80034-0.
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.
