3I8T
N-terminal CRD1 domain of mouse Galectin-4 in complex with lactose
Summary for 3I8T
| Entry DOI | 10.2210/pdb3i8t/pdb |
| Related PRD ID | PRD_900008 |
| Descriptor | Galectin-4, beta-D-galactopyranose-(1-4)-alpha-D-glucopyranose, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | s-type lectin, carbohydrate binding, molecular recognition, lectin, sugar binding protein |
| Biological source | Mus musculus (mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 19441.92 |
| Authors | Brynda, J.,Krejcirikova, V.,Rezacova, P. (deposition date: 2009-07-10, release date: 2011-02-23, Last modification date: 2023-09-06) |
| Primary citation | Krejcirikova, V.,Pachl, P.,Fabry, M.,Maly, P.,Rezacova, P.,Brynda, J. Structure of the mouse galectin-4 N-terminal carbohydrate-recognition domain reveals the mechanism of oligosaccharide recognition Acta Crystallogr.,Sect.D, 67:204-211, 2011 Cited by PubMed 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. PubMed: 21358051DOI: 10.1107/S0907444911004082 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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