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4UW5

Human galectin-7 in complex with a galactose based dendron D2-2.

Summary for 4UW5
Entry DOI10.2210/pdb4uw5/pdb
Related4UW3 4UW4 4UW6
DescriptorHUMAN GALECTIN-7, DENDRON D2-1 (3 entities in total)
Functional Keywordssugar binding protein, lectin, dendrimers, multivalency, carbohydrate binding
Biological sourceHOMO SAPIENS (HUMAN)
Cellular locationCytoplasm : P47929
Total number of polymer chains6
Total formula weight93256.69
Authors
Ramaswamy, S.,Sleiman, M.H.,Masuyer, G.,Arbez-Gindre, C.,Micha-Screttas, M.,Calogeropoulou, T.,Steele, B.R.,Acharya, K.R. (deposition date: 2014-08-08, release date: 2014-11-12, Last modification date: 2024-01-10)
Primary citationRamaswamy, S.,Haj Sleiman, M.,Masuyer, G.,Arbez-Gindre, C.,Micha-Screttas, M.,Calogeropoulou, T.,Steele, B.R.,Acharya, K.R.
Structural Basis of Multivalent Galactose-Based Dendrimer Recognition by Human Galectin-7.
FEBS J., 282:372-, 2015
Cited by
PubMed Abstract: Galectins are evolutionarily conserved and ubiquitously present animal lectins with a high affinity for β-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.
PubMed: 25367374
DOI: 10.1111/FEBS.13140
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.04 Å)
Structure validation

226707

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