Galectin-10: a new structural type of prototype galectin dimer and effects on saccharide ligand binding

Glycobiology
Jiyong SuYifa Zhou

Abstract

Galectin-10 (Gal-10) which forms Charcot-Leyden crystals in vivo, is crucial to regulating lymph cell function. Here, we solved the crystal structures of Gal-10 and eight variants at resolutions of 1.55-2.00 Å. Structural analysis and size exclusion chromatography demonstrated that Gal-10 dimerizes with a novel global shape that is different from that of other prototype galectins (e.g., Gal-1, -2 and -7). In the Gal-10 dimer, Glu33 from one subunit modifies the carbohydrate-binding site of another, essentially inhibiting disaccharide binding. Nevertheless, glycerol (and possibly other small hydroxylated molecules) can interact with residues at the ligand binding site, with His53 being the most crucial for binding. Alanine substitution of the conserved Trp residue (Trp72) that is crucial to saccharide binding in other galectins, actually leads to enhanced erythrocyte agglutination, suggesting that Trp72 negatively regulates Gal-10 ligand binding. Overall, our crystallographic and biochemical results provide insight into Gal-10 ligand binding specificity.

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Citations

Apr 10, 2020·Journal of Leukocyte Biology·Peter F WellerRossana C N Melo
Nov 15, 2018·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Jiyong Su
Jan 27, 2020·The Journal of Allergy and Clinical Immunology·Milica M GrozdanovicSteven J Ackerman
May 1, 2020·Developmental and Comparative Immunology·Gerardo R Vasta, Jin-Xing Wang
Oct 5, 2020·Biochimica Et Biophysica Acta. General Subjects·Yunlong SiJiyong Su
Nov 19, 2020·Molecular Aspects of Medicine·Lei WanFu-Tong Liu
Jul 28, 2021·International Journal of Biological Macromolecules·Baolan WuFang Han

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