5XRL

Galectin-10/Charcot-Leyden crystal protein variant N65A crystal structure

5XRL の概要

• エントリーDOI: 10.2210/pdb5xrl/pdb
• 分子名称: Galectin-10, GLYCEROL (3 entities in total)
• 機能のキーワード: galectin-10/charcot-leyden crystal protein, protein binding
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm, cytosol : Q05315
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16803.18

構造登録者

Su, J. (登録日: 2017-06-08, 公開日: 2018-01-24, 最終更新日: 2024-03-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.004 Å)