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Publication Abstract from PubMed

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 A 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 microM) and a low-affinity site with K(d2) = 28 +/- 10 mM.

Structure of the mouse galectin-4 N-terminal carbohydrate-recognition domain reveals the mechanism of oligosaccharide recognition.,Krejcirikova V, Pachl P, Fabry M, Maly P, Rezacova P, Brynda J Acta Crystallogr D Biol Crystallogr. 2011 Mar;67(Pt 3):204-11. Epub 2011, Feb 15. PMID:21358051^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.