Title : Four crystal structures of human
LLT1 , a ligand of human
NKR-P1 , in varied glycosylation and oligomerization states
Abstract :
- Human LLT1 is a C -type le ctin-like ligand of NKR-P1 ( CD161 , gene KLRB1 ), 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 first N-acetylglucosamine unit in two forms and hexameric with homogeneous GlcNAc2Man5 glycosylation.
- 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