ArticleThe Journal of biological chemistry2011
Rigid-body ligand recognition drives cytotoxic T-lymphocyte antigen 4 (CTLA-4) receptor triggering.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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The trial behind it
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
31 citing papers in PubMed, 53 citations in OpenAlex.
- Immune Checkpoint-Based Therapies in Colorectal Cancer-Current Approaches and Future Perspectives.International journal of molecular sciences · 2026Review
- Review
- Advances in Psoriasis Research: Decoding Immune Circuits and Developing Novel Therapies.International journal of molecular sciences · 2025Review
- Phenotypic and targeted drug discovery in immune therapeutics: challenges, opportunities, and future directions.RSC advances · 2025Review
- Negative Immune Checkpoint Inhibitors.Pharmaceutics · 2025Review
- The Structural Biology of T-Cell Antigen Detection at Close Contacts.Immunological reviews · 2025Review
- Post-translational modifications of immune checkpoints: unlocking new potentials in cancer immunotherapy.Experimental hematology & oncology · 2025Review
- Beyond monotherapy: multimodal strategies integrating immune checkpoint inhibitors in lymphoma management.Frontiers in immunology · 2025Review
- Evolving understanding of autoimmune mechanisms and new therapeutic strategies of autoimmune disorders.Signal transduction and targeted therapy · 2024Review
- Rigid, bivalent CTLA-4 binding to CD80 is required to disrupt the cis CD80/PD-L1 interaction.Cell reports · 2024Article
- Development of an Albumin-Masked mutPD-1Ig as a Tumor Lesion-Selective Immune Checkpoint Inhibitor.ACS omega · 2023Article
- High-yield genome engineering in primary cells using a hybrid ssDNA repair template and small-molecule cocktails.Nature biotechnology · 2023Article
- A lesion-selective albumin-CTLA4Ig as a safe and effective treatment for collagen-induced arthritis.Inflammation and regeneration · 2023Article
- Rational Strategy for Designing Peptidomimetic Small Molecules Based on Cyclic Peptides Targeting Protein-Protein Interaction between CTLA-4 and B7-1.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Differences in CD80 and CD86 transendocytosis reveal CD86 as a key target for CTLA-4 immune regulation.Nature immunology · 2022Article
- Immune Checkpoint Receptors Signaling in T Cells.International journal of molecular sciences · 2022Review
- Trapping or slowing the diffusion of T cell receptors at close contacts initiates T cell signaling.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- CTLA-4 in Regulatory T Cells for Cancer Immunotherapy.Cancers · 2021Review
- Targeting co-stimulatory molecules in autoimmune disease.Nature reviews. Drug discovery · 2020Review
- Computational insights into O-glycosylation in a CTLA4 Fc-fusion protein linker and its impact on protein quality attributes.Computational and structural biotechnology journal · 2020Article
Corrections and comments
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Authors and funding
12 authors at 8 institutions in 4 countries.
Funding
Abstract
The inhibitory T-cell surface-expressed receptor, cytotoxic T lymphocyte-associated antigen-4 (CTLA-4), which belongs to the class of cell surface proteins phosphorylated by extrinsic tyrosine kinases that also includes antigen receptors, binds the related ligands, B7-1 and B7-2, expressed on antigen-presenting cells. Conformational changes are commonly invoked to explain ligand-induced "triggering" of this class of receptors. Crystal structures of ligand-bound CTLA-4 have been reported, but not the apo form, precluding analysis of the structural changes accompanying ligand binding. The 1.8-Å resolution structure of an apo human CTLA-4 homodimer emphasizes the shared evolutionary history of the CTLA-4/CD28 subgroup of the immunoglobulin superfamily and the antigen receptors. The ligand-bound and unbound forms of both CTLA-4 and B7-1 are remarkably similar, in marked contrast to B7-2, whose binding to CTLA-4 has elements of induced fit. Isothermal titration calorimetry reveals that ligand binding by CTLA-4 is enthalpically driven and accompanied by unfavorable entropic changes. The similarity of the thermodynamic parameters determined for the interactions of CTLA-4 with B7-1 and B7-2 suggests that the binding is not highly specific, but the conformational changes observed for B7-2 binding suggest some level of selectivity. The new structure establishes that rigid-body ligand interactions are capable of triggering CTLA-4 phosphorylation by extrinsic kinase(s).
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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.