ArticleThe Journal of biological chemistry2011
Crystal structure of Fcγ receptor I and its implication in high affinity γ-immunoglobulin binding.
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 47 papers.
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Who cites it
47 citing papers in PubMed, 88 citations in OpenAlex.
- Article
- Preclinical assessment of two FcγRI-specific antibodies that competitively inhibit immune complex-FcγRI binding to suppress autoimmune responses.Nature communications · 2025Article
- A Comprehensive Review of Fc Gamma Receptors and Their Role in Systemic Lupus Erythematosus.International journal of molecular sciences · 2025Review
- Fc-FcγRI Complexes: Molecular Dynamics Simulations Shed Light on Ectodomain D3's Potential Role in IgG Binding.ACS omega · 2024Article
- Identification of CD64 as a marker for the destructive potential of synovitis in osteoarthritis.Rheumatology (Oxford, England) · 2024Article
- Site-Specific Glycosylation Analysis of Murine and Human Fcγ Receptors Reveals High Heterogeneity at ConservedJournal of proteome research · 2024Article
- Article
- Profiling the Biophysical Developability Properties of Common IgG1 Fc Effector Silencing Variants.Antibodies (Basel, Switzerland) · 2023Article
- Physiological and transcriptomic analysis dissects the molecular mechanism governing meat quality during postmortem aging in Hu sheep (Frontiers in nutrition · 2023Article
- The solution structure of the unbound IgG Fc receptor CD64 resembles its crystal structure: Implications for function.PloS one · 2023Article
- FcγRI FG-loop functions as a pH sensitive switch for IgG binding and release.Frontiers in immunology · 2023Article
- Characterization of FcγRIa (CD64) as a Ligand Molecule for Site-Specific IgG1 Capture: A Side-By-Side Comparison with Protein A.Langmuir : the ACS journal of surfaces and colloids · 2022Article
- Targeting the high affinity receptor, FcγRI, in autoimmune disease, neuropathy, and cancer.Immunotherapy advances · 2022Review
- Antibody:CD47 ratio regulates macrophage phagocytosis through competitive receptor phosphorylation.Cell reports · 2021Article
- On the Use of Surface Plasmon Resonance Biosensing to Understand IgG-FcγR Interactions.International journal of molecular sciences · 2021Review
- Article
- Dataset from HDX-MS Studies of IgG1 Glycoforms and Their Interactions with the FcγRIa (CD64) Receptor.Journal of research of the National Institute of Standards and Technology · 2021Article
- CD47 Ligation Repositions the Inhibitory Receptor SIRPA to Suppress Integrin Activation and Phagocytosis.Immunity · 2020Article
- Polymorphisms in Fc Gamma Receptors and Susceptibility to Malaria in an Endemic Population.Frontiers in immunology · 2020Review
- Size-Dependent Segregation Controls Macrophage Phagocytosis of Antibody-Opsonized Targets.Cell · 2018Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Fcγ receptors (FcγRs) play critical roles in humoral and cellular immune responses through interactions with the Fc region of immunoglobulin G (IgG). Among them, FcγRI is the only high affinity receptor for IgG and thus is a potential target for immunotherapy. Here we report the first crystal structure of an FcγRI with all three extracellular Ig-like domains (designated as D1, D2, and D3). The structure shows that, first, FcγRI has an acute D1-D2 hinge angle similar to that of FcεRI but much smaller than those observed in the low affinity Fcγ receptors. Second, the D3 domain of FcγRI is positioned away from the putative IgG binding site on the receptor and is thus unlikely to make direct contacts with Fc. Third, the replacement of FcγRIII FG-loop ((171)LVGSKNV(177)) with that of FcγRI ((171)MGKHRY(176)) resulted in a 15-fold increase in IgG(1) binding affinity, whereas a valine insertion in the FcγRI FG-loop ((171)MVGKHRY(177)) abolished the affinity enhancement. Thus, the FcγRI FG-loop with its conserved one-residue deletion is critical to the high affinity IgG binding. The structural results support FcγRI binding to IgG in a similar mode as its low affinity counterparts. Taken together, our study suggests a molecular mechanism for the high affinity IgG recognition by FcγRI and provides a structural basis for understanding its physiological function and its therapeutic implication in treating autoimmune diseases.
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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.