5k8y
Structure of the Mus musclus Langerin carbohydrate recognition domain
Structural highlights
FunctionCLC4K_MOUSE Calcium-dependent lectin displaying mannose-binding specificity. Induces the formation of Birbeck granules (BGs); is a potent regulator of membrane superimposition and zippering. Binds to sulfated as well as mannosylated glycans, keratan sulfate (KS) and beta-glucans. Facilitates uptake of antigens and is involved in the routing and/or processing of antigen for presentation to T cells.[1] [2] Publication Abstract from PubMedThe 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 on murine Langerin. Whereas 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. Bacterial polysaccharide specificity of the pattern recognition receptor Langerin is highly species dependent.,Hanske J, Schulze J, Aretz J, McBride R, Loll B, Schmidt H, Knirel Y, Rabsch W, Wahl MC, Paulson JC, Rademacher C J Biol Chem. 2016 Nov 30. pii: jbc.M116.751750. PMID:27903635[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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