ArticlemAbs2019
Antigen binding allosterically promotes Fc receptor recognition.
Article in mAbs, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
What it found
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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.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
51 citing papers in PubMed, 76 citations in OpenAlex.
- Article
- Key Role of Pro230 in the Hinge Region on the Architecture and Function of IgG1.Journal of medicinal chemistry · 2026Article
- Microsecond Dynamics of Fc-CD16a Recognition: Impact of Mutations, Core Fucosylation, and Fc Asymmetry.Antibodies (Basel, Switzerland) · 2026Article
- Article
- Changes in the Interaction Properties of Antibodies with Fc Receptors upon Binding to Target Antigens.Biosensors · 2025Article
- Exploring Experimental and In Silico Approaches for Antibody-Drug Conjugates in Oncology Therapies.Pharmaceuticals (Basel, Switzerland) · 2025Review
- Fc-Binding Cyclopeptide Induces Allostery from Fc to Fab: Revealed Through in Silico Structural Analysis to Anti-Phenobarbital Antibody.Foods (Basel, Switzerland) · 2025Article
- Targeted cancer treatment using a novel EGFR-specific Fc-fusion peptide based on GE11 peptide.Scientific reports · 2025Article
- The Glycosylation of Serum IgG Antibodies in Post-COVID-19 and Post-Vaccination Patients.International journal of molecular sciences · 2025Article
- Targeting the epidermal growth factor receptor using IgM antibodies: toward next generation cancer immunotherapy.Frontiers in immunology · 2025Article
- Antigen binding triggers long-range conformational changes in monoclonal antibodies.Frontiers in immunology · 2025Article
- Fc-FcγRI Complexes: Molecular Dynamics Simulations Shed Light on Ectodomain D3's Potential Role in IgG Binding.ACS omega · 2024Article
- Fc-FcγR interactions during infections: From neutralizing antibodies to antibody-dependent enhancement.Immunological reviews · 2024Review
- Article
- Factor VIII moiety of recombinant Factor VIII Fc fusion protein impacts Fc effector function and CD16Frontiers in immunology · 2024Article
- Evaluation of Molecular Simulations and Deep Learning Prediction of Antibodies' Recognition of TRBC1 and TRBC2.Antibodies (Basel, Switzerland) · 2023Article
- Effect of Fc core fucosylation and light chain isotype on IgG1 flexibility.Communications biology · 2023Article
- A subset of antibodies targeting citrullinated proteins confers protection from rheumatoid arthritis.Nature communications · 2023Article
- Biophysical Characterization of the Contribution of the Fab Region to the IgG-FcγRIIIa Interaction.Biochemistry · 2023Article
- Exploring the dual role of B cells in solid tumors: implications for head and neck squamous cell carcinoma.Frontiers in immunology · 2023Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
A key question in immunology is whether antigen recognition and Fc receptor (FcR) binding are allosterically linked. This question is also relevant for therapeutic antibody design. Antibody Fab and Fc domains are connected by flexible unstructured hinge region. Fc chains have conserved glycosylation sites at Asn297, with each conjugated to a core heptasaccharide and forming biantennary Fc glycan. The glycans modulate the Fc conformations and functions. It is well known that the antibody Fab and Fc domains and glycan affect antibody activity, but whether these elements act independently or synergistically is still uncertain. We simulated four antibody complexes: free antibody, antigen-bound antibody, FcR-bound antibody, and an antigen-antibody-FcR complex. We found that, in the antibody's "T/Y" conformation, the glycans, and the Fc domain all respond to antigen binding, with the antibody population shifting to two dominant clusters, both with the Fc-receptor binding site open. The simulations reveal that the Fc-glycan-receptor complexes also segregate into two conformational clusters, one corresponding to the antigen-free antibody-FcR baseline binding, and the other with an antigen-enhanced antibody-FcR interaction. Our study confirmed allosteric communications in antibody-antigen recognition and following FcR activation. Even though we observed allosteric communications through the IgG domains, the most important mechanism that we observed is the communication via population shift, stimulated by antigen binding and propagating to influence FcR recognition.
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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.