Abstract

NMR of a uniformly C-13-labeled carbohydrate was used to elucidate the atomic details of a sugar-protein complex. The structure of the C-13-labeled Man alpha(1-2)Man alpha(1-2)Man alpha OMe trisaccharide ligand, when bound to cyanovirin-N (CV-N), was characterized and revealed that in the complex the glycosidic linkage torsion angles between the two reducing-end mannoses are different from the free trisaccharide. Distances within the carbohydrate were employed for conformational analysis, and NOE-based distance mapping between sugar and protein revealed that Man alpha(1-2)Man alpha(1-2)Man alpha OMe is bound more intimately with its two reducing-end mannoses into the domain A binding site of CV-N than with the nonreducing end unit. Taking advantage of the C-13 spectral dispersion of C-13-labeled carbohydrates in isotope-filtered experiments is a versatile means for a simultaneous mapping of the binding interactions on both, the carbohydrate and the protein.

Published in

Journal of the American Chemical Society
2017, Volume: 139, number: 17, pages: 6210-6216
Publisher: AMER CHEMICAL SOC

UKÄ Subject classification

Structural Biology


Publication identifier

DOI: https://doi.org/10.1021/jacs.7b01929

Permanent link to this page (URI)

https://res.slu.se/id/publ/102272