Cargando…
Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states
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, dimer...
Autores principales: | Skálová, Tereza, Bláha, Jan, Harlos, Karl, Dušková, Jarmila, Koval’, Tomáš, Stránský, Jan, Hašek, Jindřich, Vaněk, Ondřej, Dohnálek, Jan |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4356368/ https://www.ncbi.nlm.nih.gov/pubmed/25760607 http://dx.doi.org/10.1107/S1399004714027928 |
Ejemplares similares
-
Structure of the human NK cell NKR-P1:LLT1 receptor:ligand complex reveals clustering in the immune synapse
por: Bláha, Jan, et al.
Publicado: (2022) -
Natural Killer Cell Activation Receptor NKp30 Oligomerization Depends on Its N-Glycosylation
por: Skořepa, Ondřej, et al.
Publicado: (2020) -
Trp–His covalent adduct in bilirubin oxidase is crucial for effective bilirubin binding but has a minor role in electron transfer
por: Kovaľ, Tomáš, et al.
Publicado: (2019) -
Crystallographic fragment screening-based study of a novel FAD-dependent oxidoreductase from Chaetomium thermophilum. Corrigendum
por: Švecová, Leona, et al.
Publicado: (2021) -
Crystallographic fragment screening-based study of a novel FAD-dependent oxidoreductase from Chaetomium thermophilum
por: Švecová, Leona, et al.
Publicado: (2021)