5XRJ

Galectin-10/Charcot-Leyden crystal protein variant H53A crystal structure

Summary for 5XRJ

• Entry DOI: 10.2210/pdb5xrj/pdb
• Descriptor: Galectin-10 (2 entities in total)
• Functional Keywords: galectin-10/charcot-leyden crystal protein, protein binding
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm, cytosol : Q05315
• Total number of polymer chains: 1
• Total formula weight: 16687.04

Authors

Su, J. (deposition date: 2017-06-08, release date: 2018-01-24, Last modification date: 2024-03-27)

Primary citation

Su, J.,Gao, J.,Si, Y.,Cui, L.,Song, C.,Wang, Y.,Wu, R.,Tai, G.,Zhou, Y.
Galectin-10: a new structural type of prototype galectin dimer and effects on saccharide ligand binding.
Glycobiology, 28:159-168, 2018

PubMed 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.

PubMed: 29293962
DOI: 10.1093/glycob/cwx107

Experimental method

X-RAY DIFFRACTION (1.9 Å)