5NF9

Structure of Galectin-3 CRD in complex with compound 2

Summary for 5NF9

• Entry DOI: 10.2210/pdb5nf9/pdb
• Related: 5NF7
• Descriptor: Galectin-3, ~{N}-[(2~{R},3~{R},4~{R},5~{S},6~{R})-2-acetamido-6-(hydroxymethyl)-5-[(2~{S},3~{R},4~{S},5~{R},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-4-oxidanyl-oxan-3-yl]-3-methoxy-benzamide (3 entities in total)
• Functional Keywords: galectin-3 crd, cation-pi interactions, sugar binding protein
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm: P17931
• Total number of polymer chains: 1
• Total formula weight: 16975.34

Authors

Ronin, C.,Atmanene, C.,Gautier, F.M.,Djedaini Pilard, F.,Teletchea, S.,Ciesielski, F.,Vivat Hannah, V.,Grandjean, C. (deposition date: 2017-03-13, release date: 2017-06-21, Last modification date: 2024-01-17)

Primary citation

Atmanene, C.,Ronin, C.,Teletchea, S.,Gautier, F.M.,Djedaini-Pilard, F.,Ciesielski, F.,Vivat, V.,Grandjean, C.
Biophysical and structural characterization of mono/di-arylated lactosamine derivatives interaction with human galectin-3.
Biochem. Biophys. Res. Commun., 489:281-286, 2017

PubMed Abstract: Combination of biophysical and structural techniques allowed characterizing and uncovering the mechanisms underlying increased binding affinity of lactosamine derivatives for galectin 3. In particular, complementing information gathered from X-ray crystallography, native mass spectrometry and isothermal microcalorimetry showed favorable enthalpic contribution of cation-π interaction between lactosamine aryl substitutions and arginine residues from the carbohydrate recognition domain, which resulted in two log increase in compound binding affinity. This incrementing strategy allowed individual contribution of galectin inhibitor moieties to be dissected. Altogether, our results suggest that core and substituents of these saccharide-based inhibitors can be optimized separately, providing valuable tools to study the role of galectins in diseases.

PubMed: 28554839
DOI: 10.1016/j.bbrc.2017.05.150

Experimental method

X-RAY DIFFRACTION (1.87 Å)