Structural Studies of Mouse Galectin-4 N-Terminal Domain

Galectins are an evolutionarily conserved family of 15 different lectins found in various combinations in virtually every type of animal cell. Galectins are defined as a family of β-galactoside binding proteins which are characterized by the presence of a carbohydrate recognition domain (CRD). Although galectins have not signal sequence for their transferring through the membrane, they can be externalized across the membrane by non-classical secretory pathways. Recent studies demonstrated that galectins participate in many biological processes, such as cell adhesion, cell cycle control, apoptosis, signal transduction, immune response and malignity. Based on a basic domain structure (~130 aa) , the galectin family can be divided into a prototype monovalent monomer or dimer subfamily (galectin-1, -2, -5, -7, -10, -11, -13 and 14), chimera type members (galectin-3 and -15) and tandem-repeat subfamily (galectin-4, -6, 8, -9, and -12) [1].