5K8Y

Structure of the Mus musclus Langerin carbohydrate recognition domain

Summary for 5K8Y

• Entry DOI: 10.2210/pdb5k8y/pdb
• Descriptor: C-type lectin domain family 4 member K, CALCIUM ION, HEXAETHYLENE GLYCOL, ... (5 entities in total)
• Functional Keywords: c-type lectin, glycoprotein, carbohydrate binding protein, calcium binding, crd domain, lectin, immune system
• Biological source: Mus musculus (Mouse)
• Cellular location: Membrane; Single-pass type II membrane protein: Q8VBX4
• Total number of polymer chains: 2
• Total formula weight: 36086.40

Authors

Loll, B.,Aretz, J.,Rademacher, C.,Wahl, M.C. (deposition date: 2016-05-31, release date: 2016-12-07, Last modification date: 2024-10-16)

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

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)