6K2Y
Human Galectin-14
Summary for 6K2Y
| Entry DOI | 10.2210/pdb6k2y/pdb |
| Descriptor | Placental protein 13-like (2 entities in total) |
| Functional Keywords | human galectin-14, sugar binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 32786.00 |
| Authors | |
| Primary citation | Si, Y.,Li, Y.,Yang, T.,Li, X.,Ayala, G.J.,Mayo, K.H.,Tai, G.,Su, J.,Zhou, Y. Structure-function studies of galectin-14, an important effector molecule in embryology. Febs J., 288:1041-1055, 2021 Cited by PubMed Abstract: The expression of prototype galectin-14 (Gal-14) in human placenta is higher than any other galectin, suggesting that it may play a role in fetal development and regulation of immune tolerance during pregnancy. Here, we solved the crystal structure of dimeric Gal-14 and found that its global fold is significantly different from that of other galectins with two β-strands (S5 and S6) extending from one monomer and contributing to the carbohydrate-binding domain of the other. The hemagglutination assay showed that this lectin could induce agglutination of chicken erythrocytes, even though lactose could not inhibit Gal-14-induced agglutination activity. Calorimetry indicates that lactose does not interact with this lectin. Compared to galectin-1, galectin-3, and galectin-8, Gal-14 has two key amino acids (a histidine and an arginine) in the normally conserved, canonical sugar-binding site, which are substituted by glutamine (Gln53) and histidine (His57), thus likely explaining why lactose binding to this lectin is very weak. Lactose was observed in the ligand-binding site of one Gal-14 structure, most likely because ligand binding is weak and crystals were allowed to grow over a long period of time in the presence of lactose. We also found that EGFP-tagged Gal-14 is primarily localized within the nucleus of different cell types. In addition, Gal-14 colocalized with c-Rel (a member of NF-κB family) in HeLa cells. These findings indicate that Gal-14 might regulate signal transduction pathways through NF-κB hubs. Overall, the present study provides impetus for further research into the function of Gal-14 in embryology. PubMed: 32525264DOI: 10.1111/febs.15441 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.57 Å) |
Structure validation
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