title: Structure of the mouse galectin-4 N-terminal carbohydrate-recognition domain reveals the mechanism of oligosaccharide recognition.
abstract: Galectin-4, a member of the tandem-repeat subfamily of galectins, participates in cell-membrane interactions and plays an important role in cell adhesion and modulation of immunity and malignity. The oligosaccharide specificity of the mouse galectin-4 carbohydrate-recognition domains (CRDs) has been reported previously. In this work, the structure and binding properties of the N-terminal domain CRD1 were further investigated and the crystal structure of CRD1 in complex with lactose was determined at 2.1 Å resolution. The lactose-binding affinity was characterized by fluorescence measurements and two lactose-binding sites were identified: a high-affinity site with a K(d) value in the micromolar range (K(d1) = 600 ± 70 µM) and a low-affinity site with K(d2) = 28 ± 10 mM.
authors.affiliation: Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, vvi, Prague, Czech Republic.
authors.forename: Veronika
authors.initials: V
authors.lastname: Krejčiříková
authors.forename: Petr
authors.initials: P
authors.lastname: Pachl
authors.forename: Milan
authors.initials: M
authors.lastname: Fábry
authors.forename: Petr
authors.initials: P
authors.lastname: Malý
authors.forename: Pavlína
authors.initials: P
authors.lastname: Rezáčová
authors.forename: Jiří
authors.initials: J
authors.lastname: Brynda
mesh_terms: D000818:Animals; D018360:Crystallography, X-Ray; D037541:Galectin 4 / Q000737:chemistry* / Q000378:metabolism; D007785:Lactose / Q000737:chemistry* / Q000378:metabolism; D008024:Ligands; D051379:Mice; D008958:Models, Molecular; D054730:Protein Interaction Domains and Motifs
chemical_list: D037541:Galectin 4; D008024:Ligands; D007785:Lactose