4GXL
The crystal structure of Galectin-8 C-CRD in complex with NDP52
Summary for 4GXL
| Entry DOI | 10.2210/pdb4gxl/pdb |
| Descriptor | Galectin-8, Peptide from Calcium-binding and coiled-coil domain-containing protein 2, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | protein-protein interaction, carbohydrate recognition, ndp52, protein binding |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cytoplasmic vesicle : O00214 Cytoplasm, perinuclear region : Q13137 |
| Total number of polymer chains | 2 |
| Total formula weight | 19225.69 |
| Authors | Li, S.,Wandel, M.P.,Li, F.,Liu, Z.,He, C.,Wu, J.,Shi, Y.,Randow, F. (deposition date: 2012-09-04, release date: 2013-05-08, Last modification date: 2024-03-20) |
| Primary citation | Li, S.,Wandel, M.P.,Li, F.,Liu, Z.,He, C.,Wu, J.,Shi, Y.,Randow, F. Sterical hindrance promotes selectivity of the autophagy cargo receptor NDP52 for the danger receptor galectin-8 in antibacterial autophagy Sci.Signal., 6:ra9-ra9, 2013 Cited by PubMed Abstract: Autophagy, the process of lysosome-dependent degradation of cytosolic components, is a mechanism by which cells selectively engulf invading pathogens to protect themselves against infection. Galectin-8, a cytosolic protein with specificity for β-galactoside-containing glycans, binds endosomal and lysosomal membranes that have been damaged, for example, by pathogens, and selectively recruits the autophagy cargo receptor NDP52 to induce autophagy. We solved the crystal structure of the NDP52-galectin-8 complex to show how NDP52 exclusively binds galectin-8 and, consequently, why other galectins do not restrict the growth of Salmonella in human cells. PubMed: 23386746DOI: 10.1126/scisignal.2003730 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.023 Å) |
Structure validation
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