ArticleProceedings of the National Academy of Sciences of the United States of America1999
Crystal structure of the HLA-Cw3 allotype-specific killer cell inhibitory receptor KIR2DL2.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 110 citations in OpenAlex.
- Recognition of Self and Viral Ligands by NK Cell Receptors.Immunological reviews · 2025Review
- Genetic Variants inFrontiers in immunology · 2021Article
- Immunomodulation of the Natural Killer Cell Phenotype and Response during HCV Infection.Journal of clinical medicine · 2020Review
- Structural basis for the recognition of nectin-like protein-5 by the human-activating immune receptor, DNAM-1.The Journal of biological chemistry · 2019Article
- Structure and flexibility of the extracellular region of the PirB receptor.The Journal of biological chemistry · 2019Article
- Two class I genes of the chicken MHC have different functions: BF1 is recognized by NK cells while BF2 is recognized by CTLs.Immunogenetics · 2018Article
- Modulation of Human Leukocyte Antigen-C by Human Cytomegalovirus Stimulates KIR2DS1 Recognition by Natural Killer Cells.Frontiers in immunology · 2017Article
- New insights about pilus formation in gut-adapted Lactobacillus rhamnosus GG from the crystal structure of the SpaA backbone-pilin subunit.Scientific reports · 2016Article
- KIR2DL2/2DL3-E(35) alleles are functionally stronger than -Q(35) alleles.Scientific reports · 2016Article
- Structure of FcγRI in complex with Fc reveals the importance of glycan recognition for high-affinity IgG binding.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Activating killer cell immunoglobulin-like receptor 2DS2 binds to HLA-A*11.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Homo-oligomerization of the activating natural killer cell receptor NKp30 ectodomain increases its binding affinity for cellular ligands.The Journal of biological chemistry · 2014Article
- Effects of Peptide on NK cell-mediated MHC I recognition.Frontiers in immunology · 2014Review
- Structural basis for recognition of cellular and viral ligands by NK cell receptors.Frontiers in immunology · 2014Review
- Natural killer cells and their receptors in multiple sclerosis.Brain : a journal of neurology · 2013Review
- Allelic variation in KIR2DL3 generates a KIR2DL2-like receptor with increased binding to its HLA-C ligand.Journal of immunology (Baltimore, Md. : 1950) · 2013Article
- Structural insights into activation of antiviral NK cell responses.Immunological reviews · 2012Review
- Diverse functionality among human NK cell receptors for the C1 epitope of HLA-C: KIR2DS2, KIR2DL2, and KIR2DL3.Frontiers in immunology · 2012Article
- Crystal structure of Fcγ receptor I and its implication in high affinity γ-immunoglobulin binding.The Journal of biological chemistry · 2011Article
- Crystal structure of leukocyte Ig-like receptor LILRB4 (ILT3/LIR-5/CD85k): a myeloid inhibitory receptor involved in immune tolerance.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Killer cell inhibitory receptors (KIR) protect class I HLAs expressing target cells from natural killer (NK) cell-mediated lysis. To understand the molecular basis of this receptor-ligand recognition, we have crystallized the extracellular ligand-binding domains of KIR2DL2, a member of the Ig superfamily receptors that recognize HLA-Cw1, 3, 7, and 8 allotypes. The structure was determined in two different crystal forms, an orthorhombic P212121 and a trigonal P3221 space group, to resolutions of 3.0 and 2.9 A, respectively. The overall fold of this structure, like KIR2DL1, exhibits K-type Ig topology with cis-proline residues in both domains that define beta-strand switching, which sets KIR apart from the C2-type hematopoietic growth hormone receptor fold. The hinge angle of KIR2DL2 is approximately 80 degrees, 14 degrees larger than that observed in KIR2DL1 despite the existence of conserved hydrophobic residues near the hinge region. There is also a 5 degrees difference in the observed hinge angles in two crystal forms of 2DL2, suggesting that the interdomain hinge angle is not fixed. The putative ligand-binding site is formed by residues from several variable loops with charge distribution apparently complementary to that of HLA-C. The packing of the receptors in the orthorhombic crystal form offers an intriguing model for receptor aggregation on the cell surface.
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