BOLD - A biological O-linked glycan database

Catherine A. Cooper*, Marc R. Wilkins, Keith L. Williams, Nicolle H. Packer

*Corresponding author for this work

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

Glycans can be O-linked to proteins via the hydroxyl group of serine, threonine, tyrosine, hydroxylysine or hydroxyproline. Sometimes the glycan is O-linked to the hydroxyl group via a phosphodiester bond. The core monosaccharide residue may be N-acetylgalactosamine, N-acetylglucosamine, galactose, glucose, fucose, mannose, xylose or arabinose. These O-linked glycans can remain as a monosaccharide, but often a complex structure is built up by stepwise addition of monosaccharides. Monosaccharides known to be added include galactose, N-acetylglucosamine, fucose, N-acetylneuraminic acid, N-glycolylneuraminic acid and 2-keto-3-deoxynonulosonic acid. O-linked glycans can also contain sulfate and phosphate residues. This leads to the possibility of the existence of numerous O-glycan structures. The biological O-linked database (BOLD) is a relational database that contains information on O-linked glycan structures, their biological sources (with a link to the SWISS-PROT protein database), the references in which the glycan was described (with a link to MEDLINE), and the methods used to determine the glycan structure. The database provides a valuable resource for glycobiology researchers interested in O-linked oligosaccharide structures that have been previously described on proteins from different species and tissues.

Original languageEnglish
Pages (from-to)3589-3598
Number of pages10
JournalElectrophoresis
Volume20
Issue number18
DOIs
Publication statusPublished - 1 Dec 1999

Keywords

  • database
  • O-glycosylation
  • oligosaccharide

Fingerprint Dive into the research topics of 'BOLD - A biological <i>O</i>-linked glycan database'. Together they form a unique fingerprint.

  • Cite this