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Structure of the mouse galectin-4 N-terminal carbohydrate-recognition domain reveals the mechanism of oligosaccharide recognition
V. Krejčiříková, P. Pachl, M. Fábry, P. Malý, P. Rezáčová, J. Brynda
Language English Country England, Great Britain
Document type Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S.
- MeSH
- Galectin 4 chemistry metabolism MeSH
- Protein Interaction Domains and Motifs MeSH
- Crystallography, X-Ray MeSH
- Lactose chemistry metabolism MeSH
- Ligands MeSH
- Models, Molecular MeSH
- Mice MeSH
- Animals MeSH
- Check Tag
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Research Support, U.S. Gov't, Non-P.H.S. MeSH
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.
Institute of Molecular Genetics Academy of Sciences of the Czech Republic vvi Prague Czech Republic
Institute of Molecular Genetics Czechoslovak Academy of Sciences Prague
References provided by Crossref.org
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