Crystal structures of the immune checkpoint protein LAG3 reveal critical binding interfaces for inhibitory antibodies and cellular ligands, such as FGL1 and MHC class II molecules. These structures provide insight into the dimeric assembly of LAG3 proteins on the surface of T cells and suggest FGL1-induced clustering as an immunomodulatory mechanism.
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References
Huard, B. et al. Characterization of the major histocompatibility complex class II binding site on LAG-3 protein. Proc. Natl Acad. Sci. USA 94, 5744–5749 (1997). A mutational mapping study that defines the binding site of MHC class II molecules on the LAG3 protein.
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This is a summary of: Luca, V. C. et al. LAG3 ectodomain structure reveals functional interfaces for ligand and antibody recognition. Nat. Immunol. https://doi.org/XXX (2022).
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Structure of LAG3 reveals key binding sites for immunomodulatory ligands. Nat Immunol 23, 1004–1005 (2022). https://doi.org/10.1038/s41590-022-01242-x
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DOI: https://doi.org/10.1038/s41590-022-01242-x