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Human LLT1 is a C-type lectin-like ligand of NKR-P1 (CD161, geneKLRB1), a C-type lectin-like receptor of natural killer cells. Using X-ray diffraction, the first experimental structures of human LLT1 were determined. Four structures of LLT1 under various conditions were determined: monomeric, dimeric deglycosylated after the firstN-acetylglucosamine unit in two forms and hexameric with homogeneous GlcNAc2Man5glycosylation. The dimeric form follows the classical dimerization mode of human CD69. The monomeric form keeps the same fold with the exception of the position of an outer part of the long loop region. The hexamer of glycosylated LLT1 consists of three classical dimers. The hexameric packing may indicate a possible mode of interaction of C-type lectin-like proteins in the glycosylated form.

Original publication




Journal article


Acta Crystallographica Section D Biological Crystallography


International Union of Crystallography (IUCr)

Publication Date





578 - 591