Exploiting Uniformly (13)C-Labeled Carbohydrates for Probing Carbohydrate-Protein Interactions by NMR Spectroscopy.
Exploiting Uniformly (13)C-Labeled Carbohydrates for Probing Carbohydrate-Protein Interactions by NMR Spectroscopy.
J Am Chem Soc. 2017 Apr 13;:
Authors: Nestor G, Anderson T, Oscarson S, Gronenborn AM
Abstract
NMR of a uniformly (13)C-labeled carbohydrate was used to elucidate the atomic details of a sugar-protein complex. The structure of the (13)C-labeled Man?(1-2)Man?(1-2)Man?OMe trisaccharide ligand when bound to cyanovirin-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?(1-2)Man?(1-2)Man?OMe is bound more intimately with its two reducing-end mannoses into the domain A binding site of CV-N than with the non-reducing end unit. Taking advantage of the (13)C spectral dispersion of (13)C-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.
PMID: 28406013 [PubMed - as supplied by publisher]
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