Breaking the limits in analyzing carbohydrate recognition by NMR: Resolving Branch-Selective Interaction of a Tetraantennary N-Glycan with lectins
Angewandte Chemie (International ed. in English) | 11 Oct 2017
A Canales, I Boos, L Perkams, L Karst, T Luber, T Karagiannis, G Dominguez, FJ Cañada, J Perez-Castells, D Häussinger, C Unverzagt and J Jimenez-Barbero
The biological recognition of complex-type N-glycans is part of many key physiological and pathological events. Despite their importance, the structural characterization of these events remains an unsolved task. The inherent flexibility of N-glycans hampers crystallization and the chemical equivalence of individual branches precludes their NMR characterization. By using a chemoenzymatically synthesized tetraantennary N-glycan conjugated to a lanthanide binding tag, the NMR signals under paramagnetic conditions discriminated all four N-acetyl lactosamine antennae with unprecedented resolution. The NMR data revealed the conformation of the N-glycan and permitted for the first time the direct identification of individual branches involved in the recognition by two N-acetyllactosamine-binding lectins, Datura stramonium seed lectin (DSL) and Ricinus Communis agglutinin (RCA120).
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