Structural basis for the recognition of complex‐type biantennary oligosaccharides by Pterocarpus angolensis lectin
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...
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Veröffentlicht in: | The FEBS journal 2006-06, Vol.273 (11), p.2407-2420 |
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Hauptverfasser: | , , , , , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 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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ISSN: | 1742-464X 1742-4658 |
DOI: | 10.1111/j.1742-4658.2006.05248.x |