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Influence of core protein sequence on glycosaminoglycan assembly
1Division of Cellular and Molecular Medicine, University of California, San Diego, La Jolla 92093-0687, USA. jesko@ucsd.edu
Current Opinion in Structural Biology
|October 1, 1996
Abstract:
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.