NMR Spectroscopy unveils new structural insights on Protein-Glycan Quinary Interactions

In the complex and crowded cellular environment, weak intrinsically transient interactions mediate the formation of dynamic protein complexes, leading to a new level of protein structure, the fifth level, dubbed as quinary structure. Researchers from the (Bio)Molecular Structure & Interactions by NMR Lab, at UCIBIO- FCT NOVA, used NMR spectroscopy to demonstrate the existence of quinary interactions between the human lectin, Galectin-3 (Gal-3) and serum glycoproteins, occurring through the Gal-3 lactose binding site. These interactions could help to co-localize Gal-3 at the cell surface, and may play a role in adhesion and signalling functions of this important lectin.

“Our work is a strong indication that glycosylation, as a ubiquitous post translational modifications PTM, can be a player in quinary structure and in the organization of the cellular environment at the molecular level”, explains Eurico Cabrita, head of the research team and professor at FCT NOVA.

The results were published in Chemistry - A European Journal, and highlighted by the Editors as a Hot Paper. Hot Papers are chosen by the Editors for their importance in a rapidly evolving field of high current interest. 

Chemistry-A Euroepan Journal
Protein-Glycan Quinary Interactions in Crowding Environment Unveiled by NMR Spectroscopy
Ana Diniz, Jorge S. Dias, Jesús Jiménez-Barbero, Filipa Marcelo and Eurico Cabrita
DOI: 10.1002/chem.201702800