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Protein Glycosylation pp 329–409Cite as

Adding The Finishing Touches: Terminal Elaborations

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Abstract

The remarkable diversity of eukaryotic N- and O-linked oligosaccharide structures is not only a consequence of the branching phenomena we described in Chapters 5 and 6, but can also result from the modification of the non-reducing termini of these branches: that is, the ends of the ‘antennae.’ In fact, it is the terminal groups of these antennae that are the ‘business end’ of major oligosaccharide-ligand interactions, such as those which occur in some intercellular adhesion events, and also between numerous pathogens and their target host cells. Exemplary are the sialic acids which are often part of the ligands for microbial invaders, and also fucosylated structures which are important in determining intraspecies variation and the migrational behaviour of leukocytes.

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  1. The Lundberg Laboratory, University of Göteborg, Box 462, S-405 30, Göteborg, Sweden

    Roslyn M. Bill M.A., D.Phil., M.R.S.C., C.Chem.

  2. Department of Biochemistry Research, The Hospital for Sick Children, 555 University Avenue, Toronto, Ontario, M5G 1X8, Canada

    Leigh Revers M.A., D.Phil.

  3. Department of Biochemistry Research, University of Dundee, The Wellcome Trust Building, Dow Street, Dundee, DD1 5EH, Scotland

    Iain B. H. Wilson B.Sc.(Hons), D.Phil., M.R.S.C., C.Chem.

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Bill, R.M., Revers, L., Wilson, I.B.H. (1998). Adding The Finishing Touches: Terminal Elaborations. In: Protein Glycosylation. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4939-0_7

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