Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states

0447370 - BTÚ 2016 RIV US eng J - Journal Article
Skálová, Tereza - Bláha, J. - Harlos, K. - Dušková, Jarmila - Koval, Tomáš - Stránský, Jan - Hašek, Jindřich - Vaněk, O. - Dohnálek, Jan
Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states.
Acta Crystallographica Section D-Biological Crystallography. Roč. 71, č. 3 (2015), s. 578-591. ISSN 1399-0047. E-ISSN 2059-7983
R&D Projects: GA MŠMT(CZ) ED1.1.00/02.0109; GA ČR GAP302/11/0855; GA ČR(CZ) GA15-15181S; GA MŠMT LG14009; GA MŠMT(CZ) EE2.3.30.0029
Institutional support: RVO:86652036 ; RVO:61389013
Keywords : LLT1 * C-type lectin-like ligand * NATURAL-KILLER-CELLS
Subject RIV: EB - Genetics ; Molecular Biology; EB - Genetics ; Molecular Biology (UMCH-V)
Impact factor: 2.512, year: 2015

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 GlcNAc(2)Man(5) 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.
Permanent Link: http://hdl.handle.net/11104/0249262