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Crosslinking of mammalian lectin (galectin-1) by complex biantennary saccharides

Nature Structural Biology volume 1, pages 863–870 (1994)Cite this article

Abstract

Galectins are β-galactoside-binding proteins that occur intra- and extracellularly in many animal tissues. They have been proposed to form networks of glycoconjugates on the cell surface, where they may modulate various cell response pathways such as growth, activation and adhesion. The high resolution X-ray crystallographic analyses of three crystal forms of bovine galectin-1 in complex with biantennary saccharides of N-acetyllactosamine type reveal infinite chains of lectin dimers cross-linked through N-acetyllactosamine units located at the end of the oligosaccharide antenna. The oligosaccharide adopts a different low energy conformation in each of the three crystal forms.

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Authors and Affiliations

  1. Laboratoire de Cristallographie et de Cristallisation des Macromolécules Biologiques, CNRS URA 1296, Secteur-Nord, 13916, Marseille, France

    Yves Bourne, Philippe Cantau & Christian Cambillau

  2. Glycoconjugates Section, Medical Research Council, Clinical Research Center, Watford Road, Harrow, Middlesex, HA1 3UJ, UK

    Barbara Bolgiano & Ten Feizi

  3. Centre for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville, Maryland, 20850, USA

    Der-Ing Liao & Osnat Herzberg

  4. Laboratoire de Chimie Biologique, CNRS UMR 111, Université des Sciences et Technologies de Lille, 59655, Villeuneuve d'Ascq Cedex, France

    Gérard Strecker

Authors
  1. Yves Bourne
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  2. Barbara Bolgiano
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  4. Gérard Strecker
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  5. Philippe Cantau
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  6. Osnat Herzberg
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  7. Ten Feizi
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  8. Christian Cambillau
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Bourne, Y., Bolgiano, B., Liao, DI. et al. Crosslinking of mammalian lectin (galectin-1) by complex biantennary saccharides. Nat Struct Mol Biol 1, 863–870 (1994). https://doi.org/10.1038/nsb1294-863

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  • DOI: https://doi.org/10.1038/nsb1294-863

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