7XAC
Dimeric structure of human galectin-7 in complex with two glycerol
Summary for 7XAC
| Entry DOI | 10.2210/pdb7xac/pdb |
| Descriptor | Galectin-7, GLYCEROL (3 entities in total) |
| Functional Keywords | sugar binding protein, apoptosis |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 30378.28 |
| Authors | Si, Y.L. (deposition date: 2022-03-17, release date: 2023-01-11, Last modification date: 2023-11-29) |
| Primary citation | Liang, Y.,Wang, Y.,Zhu, X.,Cai, J.,Shi, A.,Huang, J.,Zhu, Q.,Si, Y. Binding of Glycerol to Human Galectin-7 Expands Stability and Modulates Its Functions. Int J Mol Sci, 23:-, 2022 Cited by PubMed Abstract: Glycerol is seen in biological systems as an intermediate in lipid metabolism. In recent years, glycerol has been reported to act as a chemical chaperone to correct the conformation of proteins. Here, we investigate the role of glycerol in galectin-7 (Gal-7). The thermal shift and CD assays showed that the thermal stability of Gal-7 increased with glycerol concentration but with little secondary structure changes induced by glycerol. In addition, glycerol can inhibit Gal-7-mediated erythrocyte agglutination. We also solved the crystal structures of human Gal-7 in complex with glycerol in two different conditions. Glycerol binds at the carbohydrate-recognition binding sites of Gal-7, which indicates glycerol as a small ligand for Gal-7. Surprisingly, glycerol can bind a new pocket near the N-terminus of Gal-7, which can greatly reduce the flexibility and improve the stability of this region. Moreover, overexpression of Gal-7 decreased the intracellular triglyceride levels and increased mRNA expression of aquaporin-3 (AQP-3) when HeLa cells were incubated with glycerol. These findings indicate that Gal-7 might regulate glycerol metabolism. Overall, our results on human Gal-7 raise the perspective to systematically explore this so far unrecognized phenomenon for Gal-7 in glycerol metabolism. PubMed: 36293173DOI: 10.3390/ijms232012318 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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