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Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states
T. Skálová, J. Bláha, K. Harlos, J. Dušková, T. Koval', J. Stránský, J. Hašek, O. Vaněk, J. Dohnálek,
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Glycosylation MeSH
- Protein Structure, Quaternary MeSH
- NK Cell Lectin-Like Receptor Subfamily B chemistry genetics metabolism MeSH
- Lectins, C-Type chemistry genetics metabolism MeSH
- Humans MeSH
- Protein Multimerization * MeSH
- Receptors, Cell Surface chemistry genetics metabolism MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
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. 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.
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- $a Bláha, Jan $u Department of Biochemistry, Faculty of Science, Charles University Prague, Hlavova 8, 128 40 Praha, Czech Republic.
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