ArticleActa crystallographica. Section D, Biological crystallography2015
Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states.
Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 27 citations in OpenAlex.
- Reed-Sternberg cells express CD161 and lectin-like transcript 1 in Hodgkin lymphoma.Frontiers in medicine · 2026Article
- Targeting LLT1 as a potential immunotherapy option for cancer patients non-responsive to existing checkpoint therapies in multiple solid tumors.BMC cancer · 2024Article
- Structure of the human NK cell NKR-P1:LLT1 receptor:ligand complex reveals clustering in the immune synapse.Nature communications · 2022Article
- Protein purification strategies must consider downstream applications and individual biological characteristics.Microbial cell factories · 2022Review
- LLT1-CD161 Interaction in Cancer: Promises and Challenges.Frontiers in immunology · 2022Review
- Tumor Marker B7-H6 Bound to the Coiled Coil Peptide-Polymer Conjugate Enables Targeted Therapy by Activating Human Natural Killer Cells.Biomedicines · 2021Article
- Article
- Production of recombinant soluble dimeric C-type lectin-like receptors of rat natural killer cells.Scientific reports · 2019Article
- Lectin-like transcript 1 as a natural killer cell-mediated immunotherapeutic target for triple negative breast cancer and prostate cancer.Journal of cancer metastasis and treatment · 2019Article
- Recognition of host Clr-b by the inhibitory NKR-P1B receptor provides a basis for missing-self recognition.Nature communications · 2018Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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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