Journal
FEBS JOURNAL
Volume 282, Issue 2, Pages 372-387Publisher
WILEY
DOI: 10.1111/febs.13140
Keywords
carbohydrate binding; dendrimers; galectin-7; lectin; multivalency
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Funding
- University of Bath (UK)
- European Commission Marie-Curie Transfer of Knowledge Project [MTKD-CT-2004-014399]
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Galectins are evolutionarily conserved and ubiquitously present animal lectins with a high affinity for beta-galactose-containing oligosaccharides. To date, 15 mammalian galectins have been identified. Their involvement in cell-cell and cell-matrix interactions has highlighted their importance in signal transduction and other intracellular processes. Human galectin-7 (hGal-7) is a 15 kDa proto type galectin that forms a dimer in solution and its involvement in the stimulation and development of tumour growth has been reported. Previously, we reported the crystal structure of hGal-7 and its complex with galactose and lactose which provided insight into its molecular recognition and detailed interactions. Here, we present newly obtained high-resolution structural data on carbohydrate-based dendrons in complex with hGal-7. Our crystallographic data reveal how multivalent ligands interact with and form cross-links with these galectin molecules. Understanding how these dendrimeric compounds interact with hGal-7 would help in the design of new tools to investigate the recognition of carbohydrates by lectins.
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