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5YT4

Galectin-10 variant H53A soaked in glycerol for 5 minutes

Summary for 5YT4
Entry DOI10.2210/pdb5yt4/pdb
DescriptorGalectin-10, GLYCEROL (3 entities in total)
Functional Keywordsgalectin-10, cell adhesion
Biological sourceHomo sapiens (Human)
Cellular locationCytoplasm, cytosol : Q05315
Total number of polymer chains1
Total formula weight15966.13
Authors
Su, J. (deposition date: 2017-11-16, release date: 2018-01-24, Last modification date: 2024-03-27)
Primary citationSu, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

226707

건을2024-10-30부터공개중

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