Ontology highlight
ABSTRACT:
SUBMITTER: Skalova T
PROVIDER: S-EPMC4356368 | biostudies-literature | 2015 Mar
REPOSITORIES: biostudies-literature
Skálová Tereza T Bláha Jan J Harlos Karl K Dušková Jarmila J Koval' Tomáš T Stránský Jan J Hašek Jindřich J Vaněk Ondřej O Dohnálek Jan J
Acta crystallographica. Section D, Biological crystallography 20150226 Pt 3
Human LLT1 is a C-type lectin-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 ...[more]