Influence of core protein sequence on glycosaminoglycan assembly

Curr Opin Struct Biol. 1996 Oct;6(5):663-70. doi: 10.1016/s0959-440x(96)80034-0.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Glycosaminoglycans / chemistry*
  • Humans
  • Molecular Sequence Data
  • Molecular Structure
  • Sequence Analysis
  • Viral Core Proteins / chemistry*

Substances

  • Glycosaminoglycans
  • Viral Core Proteins

Associated data

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