ArticleProceedings of the National Academy of Sciences of the United States of America2001
Crystal structure of the human CD4 N-terminal two-domain fragment complexed to a class II MHC molecule.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.
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Who cites it
106 citing papers in PubMed, 264 citations in OpenAlex.
- Decade-long safety and function of retroviral-modified chimeric antigen receptor T cells.Science translational medicine · 2012Trial
- A human self-stimulatory CD4+ T cell antigen-presenting cell subset presents and recognizes agonistic self-antigens to sustain exponential autologous clonal expansion.Journal of immunology (Baltimore, Md. : 1950) · 2026Article
- Generation and characterization of humanized CD4 knock-in mice expressing chimeric mouse/human CD4 protein.Lab animal · 2026Article
- A guide to CAR T cell therapies: development, current status and future prospects.Nature reviews. Immunology · 2026Review
- The subset of M1-paired MHC class II conformers is critical for CD4+ T cell activation.Journal of immunology (Baltimore, Md. : 1950) · 2026Article
- CD4 Molecule Plays an Important Role in the Inflammatory Response Induced by Japanese Encephalitis Virus Infection.Veterinary sciences · 2026Article
- Emerging new immune checkpoint inhibitors in solid tumor immunotherapy.Naunyn-Schmiedeberg's archives of pharmacology · 2025Review
- Zinc-mediated dynamics of CD4/CD8α co-receptors and Lck kinase: implications for zinc homeostasis, immune response, and biotechnological innovations.Metallomics : integrated biometal science · 2025Review
- LAG Time in the Era of Immunotherapy-New Molecular Insights Into the Immunosuppression Mechanism of Lymphocyte Activation Gene-3.Immunological reviews · 2025Review
- Biophysical and Structural Features of αβT-Cell Receptor Mechanosensing: A Paradigmatic Shift in Understanding T-Cell Activation.Immunological reviews · 2025Review
- Deciphering LAG-3: unveiling molecular mechanisms and clinical advancements.Biomarker research · 2024Review
- Structural basis for mouse LAG3 interactions with the MHC class II molecule I-ANature communications · 2024Article
- The quantum model of T-cell activation: Revisiting immune response theories.Scandinavian journal of immunology · 2024Article
- High-throughput virtual search of small molecules for controlling the mechanical stability of human CD4.The Journal of biological chemistry · 2024Article
- Lymphocyte activation gene 3 served as a potential prognostic and immunological biomarker across various cancer types: a clinical and pan-cancer analysis.Clinical & translational immunology · 2024Article
- Targeting LAG-3, TIM-3, and TIGIT for cancer immunotherapy.Journal of hematology & oncology · 2023Review
- Role of Next Generation Immune Checkpoint Inhibitor (ICI) Therapy in Philadelphia Negative Classic Myeloproliferative Neoplasm (MPN): Review of the Literature.International journal of molecular sciences · 2023Review
- A survey of the adaptive immune genes of the polka-dot batfish Ogcocephalus cubifrons.BMC immunology · 2023Article
- Evolutionarily conserved amino acids in MHC-II mediate bat influenza A virus entry into human cells.PLoS biology · 2023Article
- LAG-3 Inhibitors: Novel Immune Checkpoint Inhibitors Changing the Landscape of Immunotherapy.Biomedicines · 2023Review
46 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The structural basis of the interaction between the CD4 coreceptor and a class II major histocompatibility complex (MHC) is described. The crystal structure of a complex containing the human CD4 N-terminal two-domain fragment and the murine I-A(k) class II MHC molecule with associated peptide (pMHCII) shows that only the "top corner" of the CD4 molecule directly contacts pMHCII. The CD4 Phe-43 side chain extends into a hydrophobic concavity formed by MHC residues from both alpha 2 and beta 2 domains. A ternary model of the CD4-pMHCII-T-cell receptor (TCR) reveals that the complex appears V-shaped with the membrane-proximal pMHCII at the apex. This configuration excludes a direct TCR-CD4 interaction and suggests how TCR and CD4 signaling is coordinated around the antigenic pMHCII complex. Human CD4 binds to HIV gp120 in a manner strikingly similar to the way in which CD4 interacts with pMHCII. Additional contacts between gp120 and CD4 give the CD4-gp120 complex a greater affinity. Thus, ligation of the viral envelope glycoprotein to CD4 occludes the pMHCII-binding site on CD4, contributing to immunodeficiency.
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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.