Beschreibung
Galectins are a family of beta-galactoside-binding proteins located in a wide range of organisms, where they exert functions that can be mediated by carbohydrate-protein and protein-protein interactions. Using a protein engineering approach, galectin-3 constructs were produced and set to perform structural studies, which allowed to ascertain the position of key amino acids in the N-terminal playing fundamental roles in galectin-3 function, like apoptosis and metastasis. On the other hand, a comprehensive genetic mapping of the galectin family identified one particular Galectin-Related Protein located in bone marrow that has a high degree of sequence identity with galectins, sharing their jelly-roll characteristic folding. Interestingly, GRP does not bind beta-galactosides. In order to study in detail the entirety of the galectin family for themes of divergence and recognition within a limited number of proteins, G. gallus GRP was chosen as model. This protein's structural resolution showed the particular hallmarks that hinder beta-galactoside binding.
Autorenporträt
Andrea Flores-Ibarra, PhD in Biomolecular Sciences, Autonomous University of Madrid. Master's Degree in Biomedical Physics, Complutense University of Madrid. Honors Bachelor's Degree in Medicinal Chemistry, Autonomous University of Puebla. Marie S. Curie Alumni Association.
