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<jats:p>Human LLT1 is a C-type lectin-like ligand of NKR-P1 (CD161, gene<jats:italic>KLRB1</jats:italic>), 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<jats:italic>N</jats:italic>-acetylglucosamine unit in two forms and hexameric with homogeneous GlcNAc<jats:sub>2</jats:sub>Man<jats:sub>5</jats:sub>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.</jats:p>

Original publication

DOI

10.1107/s1399004714027928

Type

Journal article

Journal

Acta Crystallographica Section D Biological Crystallography

Publisher

International Union of Crystallography (IUCr)

Publication Date

01/03/2015

Volume

71

Pages

578 - 591