ArticleThe Journal of biological chemistry2008
Molecular architecture of the major histocompatibility complex class I-binding site of Ly49 natural killer cell receptors.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 52 citations in OpenAlex.
- Antibody Blockade of Ly49/MHC-I interactions enhances Innate and Adaptive Immunity Against Cancer Metastasis.bioRxiv : the preprint server for biology · 2026Article
- Ly49G, but not Ly49C/I, is dispensable for diverse antigen-specific memory NK cell responses in H-2d and H-2b mice.Journal of immunology (Baltimore, Md. : 1950) · 2025Article
- H2-K1 protects murineHaematologica · 2025Article
- Recognition of Self and Viral Ligands by NK Cell Receptors.Immunological reviews · 2025Review
- Structural Models for Roseolovirus U20 And U21: Non-Classical MHC-I Like Proteins From HHV-6A, HHV-6B, and HHV-7.Frontiers in immunology · 2022Review
- Licensing Natural Killers for Antiviral Immunity.Pathogens (Basel, Switzerland) · 2021Review
- Dynamics of MHC-I molecules in the antigen processing and presentation pathway.Current opinion in immunology · 2021Review
- Structure of MHC class I-like MILL2 reveals heparan-sulfate binding and interdomain flexibility.Nature communications · 2018Article
- Listeria monocytogenes infection enhances the interaction between rat non-classical MHC-Ib molecule and Ly49 receptors.Innate immunity · 2018Article
- Major Histocompatibility Complex (MHC) Class I and MHC Class II Proteins: Conformational Plasticity in Antigen Presentation.Frontiers in immunology · 2017Review
- Recognition of the Major Histocompatibility Complex (MHC) Class Ib Molecule H2-Q10 by the Natural Killer Cell Receptor Ly49C.The Journal of biological chemistry · 2016Article
- Co-evolution of MHC class I and variable NK cell receptors in placental mammals.Immunological reviews · 2015Review
- Identities of P2 and P3 Residues of H-2Kb-Bound Peptides Determine Mouse Ly49C Recognition.PloS one · 2015Article
- Antigen-specific expansion and differentiation of natural killer cells by alloantigen stimulation.The Journal of experimental medicine · 2014Article
- The activating Ly49W and inhibitory Ly49G NK cell receptors display similar affinities for identical MHC class I ligands.Immunogenetics · 2014Article
- A positive cooperativity binding model between Ly49 natural killer cell receptors and the viral immunoevasin m157: kinetic and thermodynamic studies.The Journal of biological chemistry · 2014Article
- Structural basis for recognition of cellular and viral ligands by NK cell receptors.Frontiers in immunology · 2014Review
- Peptide modulation of class I major histocompatibility complex protein molecular flexibility and the implications for immune recognition.The Journal of biological chemistry · 2013Article
- Structure of NKp65 bound to its keratinocyte ligand reveals basis for genetically linked recognition in natural killer gene complex.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Targeting of a natural killer cell receptor family by a viral immunoevasin.Nature immunology · 2013Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Natural killer (NK) cells play a vital role in the detection and destruction of virally infected and tumor cells during innate immune responses. The highly polymorphic Ly49 family of NK receptors regulates NK cell function by sensing major histocompatibility complex class I (MHC-I) molecules on target cells. Despite the determination of two Ly49-MHC-I complex structures, the molecular features of Ly49 receptors that confer specificity for particular MHC-I alleles have not been identified. To understand the functional architecture of Ly49-binding sites, we determined the crystal structures of Ly49C and Ly49G and completed refinement of the Ly49C-H-2K(b) complex. This information, combined with mutational analysis of Ly49A, permitted a structure-based classification of Ly49s that we used to dissect the binding site into three distinct regions, each having different roles in MHC recognition. One region, located at the center of the binding site, has a similar structure across the Ly49 family and mediates conserved interactions with MHC-I that contribute most to binding. However, the preference of individual Ly49s for particular MHC-I molecules is governed by two regions that flank the central region and are structurally more variable. One of the flanking regions divides Ly49s into those that recognize both H-2D and H-2K versus only H-2D ligands, whereas the other discriminates among H-2D or H-2K alleles. The modular design of Ly49-binding sites provides a framework for predicting the MHC-binding specificity of Ly49s that have not been characterized experimentally.
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