5DG2

Sugar binding protein - human galectin-2 (dimer)

5DG2 の概要

• エントリーDOI: 10.2210/pdb5dg2/pdb
• 関連するPDBエントリー: 5DG1
• 関連するBIRD辞書のPRD_ID: PRD_900008
• 分子名称: Galectin-2, beta-D-galactopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
• 機能のキーワード: human galectin-2, sugar binding protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30233.75

構造登録者

Su, J.Y.,Si, Y.L. (登録日: 2015-08-27, 公開日: 2016-09-14, 最終更新日: 2023-11-08)

主引用文献

Si, Y.,Feng, S.,Gao, J.,Wang, Y.,Zhang, Z.,Meng, Y.,Zhou, Y.,Tai, G.,Su, J.
Human galectin-2 interacts with carbohydrates and peptides non-classically: new insight from X-ray crystallography and hemagglutination.
Acta Biochim. Biophys. Sin. (Shanghai), 48:939-947, 2016

PubMed Abstract: Galectin-2 (Gal-2) plays a role in cancer, myocardial infarction, immune response, and gastrointestinal tract diseases. The only reported crystal structure of Gal-2 shows that it is a dimer in which the monomer subunits have almost identical structures, each binding with one molecule of lactose. In this study, we crystallized Gal-2 under new conditions that produced three crystal structures. In each Gal-2 dimer structure, lactose was shown to be bound to only one of the carbohydrate recognition domain subunits. In solution studies, the thermal shift assay demonstrated that inequivalent monomer subunits in the Gal-2 dimer become equivalent upon ligand binding. In addition, galectin-mediated erythrocyte agglutination assays using lactose and larger complex polysaccharides as inhibitors showed the structural differences between Gal-1 and Gal-2. Overall, our results reveal some novel aspects to the structural differentiation in Gal-2 and expand the potential for different types of molecular interactions that may be specific to this lectin.

PubMed: 27563008
DOI: 10.1093/abbs/gmw089

実験手法

X-RAY DIFFRACTION (1.612 Å)