Molecular recognition of complex-type biantennary N-glycans by protein receptors: a 3D view on epitope selection by NMR.
Related Articles Molecular recognition of complex-type biantennary N-glycans by protein receptors: a 3D view on epitope selection by NMR.
J Am Chem Soc. 2013 Jan 29;
Authors: Arda A, Blasco P, Varon Silva D, Schubert V, André S, Bruix M, Cañada FJ, Gabius HJ, Unverzagt C, Jimenez-Barbero J
Abstract
The current surge in defining glycobiomarkers by applying lectins rekindles interest in definition of the sugar-binding sites of lectins at high resolution. Natural complex-type N-glycans can present more than one potential binding motif, posing the question of the actual mode of interaction when interpreting e.g. lectin array data. By strategically combining N-glycan preparation with STD NMR and modeling, we illustrate that epitope recognition depends on the structural context of both the sugar and the lectin (here, wheat germ agglutinin and a single hevein domain), and cannot always be predicted from simplified model systems studied in the solid state. We also monitor branch-end substitutions by this strategy and describe a 3D structure which accounts for the accommodation of the a2,6 sialylated terminus of a biantennary N-glycan by viscumin. In addition, we provide a structural explanation for the role of terminal a2,6-sialylation in precluding the interaction of natural N-glycans with lectind from Maackia amurensis. The approach described is thus capable of pinpointing lectin-binding motifs in natural N-glycans and providing detailed structural explanations for lectin selectivity.
PMID: 23360551 [PubMed - as supplied by publisher]
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