Structural basis for the recognition of complex-type biantennary oligosaccharides by Pterocarpus angolensis lectin

Authors

  • Lieven Buts,

    1.  Laboratorium voor Ultrastructuur, Vrije Universiteit Brussel and Department of Molecular and Cellular Interactions, Vlaams Interuniversitair Instituut voor Biotechnologie, Belgium
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  • Abel Garcia-Pino,

    1.  Laboratorium voor Ultrastructuur, Vrije Universiteit Brussel and Department of Molecular and Cellular Interactions, Vlaams Interuniversitair Instituut voor Biotechnologie, Belgium
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  • Anne Imberty,

    1.  Centre de Recherches sur les Macromolécules Végétales (CERMAV) – CNRS (affiliated with Joseph Fourier University), Grenoble, France
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  • Nicolas Amiot,

    1.  Complex Carbohydrate Research Center, The University of Georgia, Athens, GA, USA
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  • Geert-Jan Boons,

    1.  Complex Carbohydrate Research Center, The University of Georgia, Athens, GA, USA
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  • Sonia Beeckmans,

    1.  Laboratorium voor Scheikunde der Proteïnen, Instituut voor Moleculaire Biologie, Vrije Universiteit Brussel, Belgium
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  • Wim Versées,

    1.  Laboratorium voor Ultrastructuur, Vrije Universiteit Brussel and Department of Molecular and Cellular Interactions, Vlaams Interuniversitair Instituut voor Biotechnologie, Belgium
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  • Lode Wyns,

    1.  Laboratorium voor Ultrastructuur, Vrije Universiteit Brussel and Department of Molecular and Cellular Interactions, Vlaams Interuniversitair Instituut voor Biotechnologie, Belgium
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  • Remy Loris

    1.  Laboratorium voor Ultrastructuur, Vrije Universiteit Brussel and Department of Molecular and Cellular Interactions, Vlaams Interuniversitair Instituut voor Biotechnologie, Belgium
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R. Loris, Laboratorium voor Ultrastructuur, Vrije Universiteit Brussel and Department of Molecular and Cellular Interactions, Vlaams Interuniversitair Instituut voor Biotechnologie, Pleinlaan 2, B-1050 Brussels, Belgium
Fax: +32 2 6291963
Tel: +32 2 6291989
E-mail: reloris@vub.ac.be

Abstract

The crystal structure of Pterocarpus angolensis lectin is determined in its ligand-free state, in complex with the fucosylated biantennary complex type decasaccharide NA2F, and in complex with a series of smaller oligosaccharide constituents of NA2F. These results together with thermodynamic binding data indicate that the complete oligosaccharide binding site of the lectin consists of five subsites allowing the specific recognition of the pentasaccharide GlcNAcβ(1–2)Manα(1–3)[GlcNAcβ(1–2)Manα(1–6)]Man. The mannose on the 1–6 arm occupies the monosaccharide binding site while the GlcNAc residue on this arm occupies a subsite that is almost identical to that of concanavalin A (con A). The core mannose and the GlcNAcβ(1–2)Man moiety on the 1–3 arm on the other hand occupy a series of subsites distinct from those of con A.

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