ArticleProceedings of the National Academy of Sciences of the United States of America1994
The role of charge and multiple faces of the CD8 alpha/alpha homodimer in binding to major histocompatibility complex class I molecules: support for a bivalent model.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed, 50 citations in OpenAlex.
- Uncovering immune cell heterogeneity in hepatocellular carcinoma by combining single-cell RNA sequencing with T-cell receptor sequencing.World journal of hepatology · 2025Article
- Crystallization and preliminary X-ray structural studies of a high-affinity CD8alphaalpha co-receptor to pMHC.Acta crystallographica. Section F, Structural biology and crystallization communications · 2005Article
- Sequence conservation in the chagasin family suggests a common trend in cysteine proteinase binding by unrelated protein inhibitors.Protein science : a publication of the Protein Society · 2002Article
- Molecular analysis of protein interactions mediating the function of the cell surface protein CD8.Immunologic research · 1999Review
- Assembly and crystallization of the complex between the human T cell coreceptor CD8alpha homodimer and HLA-A2.Protein science : a publication of the Protein Society · 1998Article
- Characterization of the major histocompatibility complex class II binding site on LAG-3 protein.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Glu227-->Lys substitution in the acidic loop of major histocompatibility complex class I alpha 3 domain distinguishes low avidity CD8 coreceptor and avidity-enhanced CD8 accessory functions.The Journal of experimental medicine · 1996Article
- Interaction between CD8 and major histocompatibility complex (MHC) class I mediated by multiple contact surfaces that include the alpha 2 and alpha 3 domains of MHC class I.The Journal of experimental medicine · 1995Article
- Human CD8 transgene regulation of HLA recognition by murine T cells.The Journal of experimental medicine · 1995Article
- The three-dimensional structure of a class I major histocompatibility complex molecule missing the alpha 3 domain of the heavy chain.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Production and characterization of transformed B-lymphocytes expressing the membrane defect of Scott syndrome.The Journal of clinical investigation · 1994Article
- Complementarity determining region 1 (CDR1)- and CDR3-analogous regions in CTLA-4 and CD28 determine the binding to B7-1.The Journal of experimental medicine · 1994Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The CD8 dimer interacts with the alpha 3 domain of major histocompatibility complex class I molecules through two immunoglobulin variable-like domains. In this study a crystal structure-informed mutational analysis has been performed to identify amino acids in the CD8 alpha/alpha homodimer that are likely to be involved in binding to class I. Several key residues are situated on the top face of the dimer within loops analogous to the complementarity-determining regions (CDRs) of immunoglobulin. In addition, other important amino acids are located in the A and B beta-strands on the sides of the dimer. The potential involvement of amino acids on both the top and the side faces of the molecule is consistent with a bivalent model for the interaction between a single CD8 alpha/alpha homodimer and two class I molecules and may have important implications for signal transduction in class I-expressing cells. This study also demonstrates a role for the positive surface potential of CD8 in class I binding and complements previous work demonstrating the importance of a negatively charged loop on the alpha 3 domain of class I for CD8 alpha/alpha-class I interaction. We propose a model whereby residues located on the CDR-like loops of the CD8 homodimer interact with the alpha 3 domain of MHC class I while amino acids on the side of the molecule containing the A and B beta-strands contact the alpha 2 domain of class I.
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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.