ArticleNature communications2022
Structure of the human NK cell NKR-P1:LLT1 receptor:ligand complex reveals clustering in the immune synapse.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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Who cites it
17 citing papers in PubMed, 21 citations in OpenAlex.
- NKR-P1A/CD161: A Multifunctional Immune Receptor at the Crossroads of Antitumor Immunity.Biomolecules · 2026Review
- Protease-mediated maturation of M-PMV reverse transcriptase into a functional heterodimer.Protein science : a publication of the Protein Society · 2026Article
- CD161 and LLT1 expression in immune cell populations of Hodgkin lymphoma tumor microenvironment.Frontiers in medicine · 2026Article
- MINFLUX nanoscopy to study the NK cell immune synapse.Methods in cell biology · 2026Article
- Reed-Sternberg cells express CD161 and lectin-like transcript 1 in Hodgkin lymphoma.Frontiers in medicine · 2026Article
- Peripheral γδ T-cell remodeling in psoriasis is associated with effector-biased transcriptional organization and reduced representation of a circulatingFrontiers in immunology · 2026Article
- Article
- Recognition of Self and Viral Ligands by NK Cell Receptors.Immunological reviews · 2025Review
- AI-based hardware and software tools in microscopy to boost research in immunology and virology.Frontiers in immunology · 2025Review
- Rab8a restores diverse innate functions in CD11cNature communications · 2024Article
- NK-cell receptor modulation in viral infections.Clinical and experimental immunology · 2024Review
- Lectin-like Transcript-1 (LLT1) Expression in Oral Squamous Cell Carcinomas: Prognostic Significance and Relationship with the Tumor Immune Microenvironment.International journal of molecular sciences · 2024Article
- Article
- Delineating the early dissemination mechanisms of acral melanoma by integrating single-cell and spatial transcriptomic analyses.Nature communications · 2023Article
- Small-angle X-ray scattering studies of enzymes.Current opinion in chemical biology · 2023Review
- The diverse roles of C-type lectin-like receptors in immunity.Frontiers in immunology · 2023Review
- SARS-CoV-2 infection impairs NK cell functionsFrontiers in immunology · 2023Article
Corrections and comments
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Authors and funding
17 authors at 5 institutions in 6 countries.
Funding
Abstract
Signaling by the human C-type lectin-like receptor, natural killer (NK) cell inhibitory receptor NKR-P1, has a critical role in many immune-related diseases and cancer. C-type lectin-like receptors have weak affinities to their ligands; therefore, setting up a comprehensive model of NKR-P1-LLT1 interactions that considers the natural state of the receptor on the cell surface is necessary to understand its functions. Here we report the crystal structures of the NKR-P1 and NKR-P1:LLT1 complexes, which provides evidence that NKR-P1 forms homodimers in an unexpected arrangement to enable LLT1 binding in two modes, bridging two LLT1 molecules. These interaction clusters are suggestive of an inhibitory immune synapse. By observing the formation of these clusters in solution using SEC-SAXS analysis, by dSTORM super-resolution microscopy on the cell surface, and by following their role in receptor signaling with freshly isolated NK cells, we show that only the ligation of both LLT1 binding interfaces leads to effective NKR-P1 inhibitory signaling. In summary, our findings collectively support a model of NKR-P1:LLT1 clustering, which allows the interacting proteins to overcome weak ligand-receptor affinity and to trigger signal transduction upon cellular contact in the immune synapse.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.