ArticleThe Journal of biological chemistry2015
The structure of the atypical killer cell immunoglobulin-like receptor, KIR2DL4.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 46 citations in OpenAlex.
- Article
- Recognition of Self and Viral Ligands by NK Cell Receptors.Immunological reviews · 2025Review
- ITAM-based receptors in natural killer cells.Immunological reviews · 2024Review
- Harnessing the potential of HLA-G in cancer therapy: advances, challenges, and prospects.Journal of translational medicine · 2024Review
- Article
- High-throughput virtual screening of small-molecule inhibitors targeting immune cell checkpoints to discover new immunotherapeutics for human diseases.Molecular diversity · 2023Article
- Local immune recognition of trophoblast in early human pregnancy: controversies and questions.Nature reviews. Immunology · 2023Review
- Evolution and molecular interactions of major histocompatibility complex (MHC)-G, -E and -F genes.Cellular and molecular life sciences : CMLS · 2022Review
- Roles of HLA-G/KIR2DL4 in Breast Cancer Immune Microenvironment.Frontiers in immunology · 2022Review
- Structural plasticity of KIR2DL2 and KIR2DL3 enables altered docking geometries atop HLA-C.Nature communications · 2021Article
- Decidual Natural Killer Cells: A Good Nanny at the Maternal-Fetal Interface During Early Pregnancy.Frontiers in immunology · 2021Review
- The Molecular and Functional Characteristics of HLA-G and the Interaction with Its Receptors: Where to Intervene for Cancer Immunotherapy?International journal of molecular sciences · 2020Review
- HLA-G Neo-Expression on Tumors.Frontiers in immunology · 2020Review
- The microstructure in the placenta is influenced by the functional diversity of HLA-G allelic variants.Immunogenetics · 2019Article
- European Patent in Immunoncology: From Immunological Principles of Implantation to Cancer Treatment.International journal of molecular sciences · 2019Review
- Structure and flexibility of the extracellular region of the PirB receptor.The Journal of biological chemistry · 2019Article
- Conservation, Extensive Heterozygosity, and Convergence of Signaling Potential All Indicate a Critical Role for KIR3DL3 in Higher Primates.Frontiers in immunology · 2019Article
- KIR, LILRB and their Ligands' Genes as Potential Biomarkers in Recurrent Implantation Failure.Archivum immunologiae et therapiae experimentalis · 2017Review
- Natural Killer Cell Interactions with Classical and Non-Classical Human Leukocyte Antigen Class I in HIV-1 Infection.Frontiers in immunology · 2017Review
- Uterine Natural Killer Cells: Functional Distinctions and Influence on Pregnancy in Humans and Mice.Frontiers in immunology · 2017Review
Corrections and comments
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Authors and funding
13 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The engagement of natural killer cell immunoglobulin-like receptors (KIRs) with their target ligands, human leukocyte antigen (HLA) molecules, is a critical component of innate immunity. Structurally, KIRs typically have either two (D1-D2) or three (D0-D1-D2) extracellular immunoglobulin domains, with the D1 and D2 domain recognizing the α1 and α2 helices of HLA, respectively, whereas the D0 domain of the KIR3DLs binds a loop region flanking the α1 helix of the HLA molecule. KIR2DL4 is distinct from other KIRs (except KIR2DL5) in that it does not contain a D1 domain and instead has a D0-D2 arrangement. Functionally, KIR2DL4 is also atypical in that, unlike all other KIRs, KIR2DL4 has both activating and inhibitory signaling domains. Here, we determined the 2.8 Å crystal structure of the extracellular domains of KIR2DL4. Structurally, KIR2DL4 is reminiscent of other KIR2DL receptors, with the D0 and D2 adopting the C2-type immunoglobulin fold arranged with an acute elbow angle. However, KIR2DL4 self-associated via the D0 domain in a concentration-dependent manner and was observed as a tetramer in the crystal lattice by size exclusion chromatography, dynamic light scattering, analytical ultracentrifugation, and small angle x-ray scattering experiments. The assignment of residues in the D0 domain to forming the KIR2DL4 tetramer precludes an interaction with HLA akin to that observed for KIR3DL1. Accordingly, no interaction was observed to HLA by direct binding studies. Our data suggest that the unique functional properties of KIR2DL4 may be mediated by self-association of the receptor.
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