5DG2

Sugar binding protein - human galectin-2 (dimer)

Summary for 5DG2

• Entry DOI: 10.2210/pdb5dg2/pdb
• Related: 5DG1
• Related PRD ID: PRD_900008
• Descriptor: Galectin-2, beta-D-galactopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
• Functional Keywords: human galectin-2, sugar binding protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 30233.75

Authors

Su, J.Y.,Si, Y.L. (deposition date: 2015-08-27, release date: 2016-09-14, Last modification date: 2023-11-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.612 Å)