5M62
Structure of the Mus musclus Langerin carbohydrate recognition domain in complex with glucose
Summary for 5M62
Entry DOI | 10.2210/pdb5m62/pdb |
Related | 5K8Y |
Descriptor | C-type lectin domain family 4 member K, CALCIUM ION, GLYCEROL, ... (7 entities in total) |
Functional Keywords | c-type lectin, glycoprotein, carbohydrate binding protein, calcium binding, crd domain, lectin, immune system |
Biological source | Mus musculus (Mouse) |
Total number of polymer chains | 2 |
Total formula weight | 36957.06 |
Authors | Loll, B.,Aretz, J.,Rademacher, C.,Wahl, M.C. (deposition date: 2016-10-24, release date: 2016-12-07, Last modification date: 2024-11-13) |
Primary citation | Hanske, J.,Schulze, J.,Aretz, J.,McBride, R.,Loll, B.,Schmidt, H.,Knirel, Y.,Rabsch, W.,Wahl, M.C.,Paulson, J.C.,Rademacher, C. Bacterial Polysaccharide Specificity of the Pattern Recognition Receptor Langerin Is Highly Species-dependent. J. Biol. Chem., 292:862-871, 2017 Cited by PubMed Abstract: The recognition of pathogen surface polysaccharides by glycan-binding proteins is a cornerstone of innate host defense. Many members of the C-type lectin receptor family serve as pattern recognition receptors facilitating pathogen uptake, antigen processing, and immunomodulation. Despite the high evolutionary pressure in host-pathogen interactions, it is still widely assumed that genetic homology conveys similar specificities. Here, we investigate the ligand specificities of the human and murine forms of the myeloid C-type lectin receptor langerin for simple and complex ligands augmented by structural insight into murine langerin. Although the two homologs share the same three-dimensional structure and recognize simple ligands identically, a screening of more than 300 bacterial polysaccharides revealed highly diverging avidity and selectivity for larger and more complex glycans. Structural and evolutionary conservation analysis identified a highly variable surface adjacent to the canonic binding site, potentially forming a secondary site of interaction for large glycans. PubMed: 27903635DOI: 10.1074/jbc.M116.751750 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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