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Publication Abstract from PubMed

Galectins are involved in many cellular processes due to their ability to bind carbohydrates. Understanding their functions has shown the necessity for potent and specific galectin inhibitors. Human galectin-7 (hGal-7) in particular, has been highlighted as an important marker in many types of cancer by either inhibiting or promoting tumour growth. Producing ligands able to selectively target hGal-7 will offer promising tools for deciphering cancer processes in which hGal-7 is involved as well as present potential solutions for future therapeutics. Here we report the high resolution crystal structure of hGal-7 in complex with a synthetic 2-O-benzylphosphate-galactoside inhibitor (which is >60-fold potent than its parent galactoside). The high resolution crystallographic analysis highlights the validity of using saccharide derivatives, conserving properties of the galactose binding, while enhanced affinity and specificity is provided by the added phosphate group. This structural information will allow the design of further inhibitor with improved potency and specificity. Structured digital abstract hGal-7 and hGal-7 bind by x-ray crystallography (View interaction).

Inhibition mechanism of human galectin-7 by a novel galactose-benzylphosphate inhibitor.,Masuyer G, Jabeen T, Oberg CT, Leffler H, Nilsson UJ, Acharya KR FEBS J. 2011 Nov 7. doi: 10.1111/j.1742-4658.2011.08414.x. PMID:22059385^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.