3ZXE

Crystal structure of Human Galectin-7 in complex with a galactose- benzylphosphate inhibitor

Summary for 3ZXE

• Entry DOI: 10.2210/pdb3zxe/pdb
• Related: 1BKZ 2GAL 3GAL 3ZXF 4GAL 5GAL
• Descriptor: GALECTIN-7, METHYL 2-O-[(S)-(BENZYLOXY)(HYDROXY)PHOSPHORYL]-3-DEOXY-3-{[(4-METHYLPHENYL)CARBONYL]AMINO}-1-THIO-BETA-D-GALACTOPYRANOSIDE (3 entities in total)
• Functional Keywords: sugar binding protein
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm: P47929
• Total number of polymer chains: 2
• Total formula weight: 30524.33

Authors

Masuyer, G.,Oberg, C.T.,Leffler, H.,Nilsson, U.J.,Acharya, K.R. (deposition date: 2011-08-10, release date: 2011-11-30, Last modification date: 2023-12-20)

Primary citation

Masuyer, G.,Jabeen, T.,Oberg, C.T.,Leffler, H.,Nilsson, U.J.,Acharya, K.R.
Inhibition Mechanism of Human Galectin-7 by a Novel Galactose-Benzylphosphate Inhibitor.
FEBS J., 279:193-, 2012

PubMed Abstract: 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 more 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 inhibitors with improved potency and specificity.

PubMed: 22059385
DOI: 10.1111/J.1742-4658.2011.08414.X

Experimental method

X-RAY DIFFRACTION (1.67 Å)