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Structural basis of multivalent galactose-based dendrimer recognition by human galectin-7

DOI: 10.1111/febs.13140 DOI Help
PMID: 25367374 PMID Help

Authors: Sneha Ramaswamy (Department of Biology and Biochemistry, University of Bath) , Mazen H. Sleiman (National Hellenic Research Foundation, Institute of Biology, Medicinal Chemistry and Biotechnology, Athens) , Geoffrey Masuyer (Department of Biology and Biochemistry, University of Bath) , Cécile Arbez-gindre (National Hellenic Research Foundation, Institute of Biology, Medicinal Chemistry and Biotechnology, Athens) , Maria Micha-screttas (National Hellenic Research Foundation, Institute of Biology, Medicinal Chemistry and Biotechnology, Athens) , Theodora Calogeropoulou (National Hellenic Research Foundation, Institute of Biology, Medicinal Chemistry and Biotechnology, Athens) , Barry R. Steele (National Hellenic Research Foundation, Institute of Biology, Medicinal Chemistry and Biotechnology, Athens) , Ravi Acharya (Department of Biology and Biochemistry, University of Bath)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Febs Journal , VOL 282 (2) , PAGES 372 - 387

State: Published (Approved)
Published: January 2015
Diamond Proposal Number(s): 8922

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.

Journal Keywords: carbohydrate binding; dendrimers; galectin‐7; lectin; multivalency

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography

Added On: 24/02/2015 09:07

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