Structure of the mouse galectin-4 N-terminal carbohydrate-recognition domain reveals the mechanism of oligosaccharide recognition
✍ Scribed by Krejčiříková, Veronika ;Pachl, Petr ;Fábry, Milan ;Malý, Petr ;Řezáčová, Pavlína ;Brynda, Jiří
- Publisher
- International Union of Crystallography
- Year
- 2011
- Tongue
- English
- Weight
- 870 KB
- Volume
- 67
- Category
- Article
- ISSN
- 0907-4449
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✦ Synopsis
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 AE 70 mM) and a low-affinity site with K d2 = 28 AE 10 mM.