NMR of glycoproteins: profiling, structure, conformation and interactions

• Published in: Current opinion in structural biology Vol. 68; pp. 9 - 17
• Main Authors: Unione, Luca, Ardá, Ana, Jiménez-Barbero, Jesús, Millet, Oscar
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.06.2021
• ISSN: 0959-440X; 1879-033X; 1879-033X
• DOI: 10.1016/j.sbi.2020.09.009

•NMR is most suitable for the structural characterization of glycoproteins.•Protein overexpression in eukaryotic media can produce glycoproteins at high yield and with tailored labeling conditions.•NMR in combination with computational tools provide a proper description of the structure and dynamics of glycoproteins.•The main remaining challenge is to produce glycoproteins decorated with the bioactive glycan composition. In glycoproteins, carbohydrates are responsible for the selective interaction and tight regulation of cellular processes, constituting the main information transducer interface in protein–glycoprotein interactions. Increasing experimental and computational evidence suggest that such interactions often induce allosteric changes in the host protein, underlining the importance of studying intact glycoproteins. Technical issues have precluded such studies for years but, nowadays, a promising era is emerging where NMR spectroscopy, among other techniques, allows the characterization of the composition, structure and segmental dynamics of glycoproteins. In this review, we discuss such advances and highlight some selected examples. This novel technology unravels multiple new functional mechanisms, subtly hidden within the sugar code.