4UW4

Human galectin-7 in complex with a galactose based dendron D2-1.

Summary for 4UW4

• Entry DOI: 10.2210/pdb4uw4/pdb
• Related: 4UW3 4UW5 4UW6
• Descriptor: GALECTIN-7, DENDRON D2-1 (3 entities in total)
• Functional Keywords: sugar binding protein, lectin, dendrimers, multivalency, carbohydrate binding
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 2
• Total formula weight: 31531.30

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 citation

Ramaswamy, 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

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

Experimental method

X-RAY DIFFRACTION (1.766 Å)