Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5M62

Structure of the Mus musclus Langerin carbohydrate recognition domain in complex with glucose

Summary for 5M62
Entry DOI10.2210/pdb5m62/pdb
Related5K8Y
DescriptorC-type lectin domain family 4 member K, CALCIUM ION, GLYCEROL, ... (7 entities in total)
Functional Keywordsc-type lectin, glycoprotein, carbohydrate binding protein, calcium binding, crd domain, lectin, immune system
Biological sourceMus musculus (Mouse)
Total number of polymer chains2
Total formula weight36957.06
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 citationHanske, 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: 27903635
DOI: 10.1074/jbc.M116.751750
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

229380

PDB entries from 2024-12-25

PDB statisticsPDBj update infoContact PDBjnumon