ArticleProceedings of the National Academy of Sciences of the United States of America2015
Structure of FcγRI in complex with Fc reveals the importance of glycan recognition for high-affinity IgG binding.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.
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Who cites it
98 citing papers in PubMed, 143 citations in OpenAlex.
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- Key Role of Pro230 in the Hinge Region on the Architecture and Function of IgG1.Journal of medicinal chemistry · 2026Article
- Transplacental Antibody Transfer: Mechanisms, Pregnancy-Related Disruptions, and Emerging Experimental Models.Antibodies (Basel, Switzerland) · 2026Review
- Human FcRL5 is an Fc receptor that simultaneously engages two IgGs.Science advances · 2026Article
- IgG N-glycosylation in autoimmune diseases.Frontiers in immunology · 2026Review
- Immunoglobulin germline reference sequences enable investigations and reveal insights into bat-specific immunity.iScience · 2025Article
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- Preclinical assessment of two FcγRI-specific antibodies that competitively inhibit immune complex-FcγRI binding to suppress autoimmune responses.Nature communications · 2025Article
- Through every lens: assessing the impact of chemical modifications on antibody-conjugates using in vivo imaging.Npj imaging · 2025Review
- The Crystal Structure of Human IgD-Fc Reveals Unexpected Differences With Other Antibody Isotypes.Proteins · 2025Article
- A Comprehensive Review of Fc Gamma Receptors and Their Role in Systemic Lupus Erythematosus.International journal of molecular sciences · 2025Review
- Identification and validation of an endotoxin tolerance-based prognostic model with therapeutic insights in sepsis.Frontiers in immunology · 2025Article
- Fc-FcγRI Complexes: Molecular Dynamics Simulations Shed Light on Ectodomain D3's Potential Role in IgG Binding.ACS omega · 2024Article
- Generating and characterizing a comprehensive panel of CHO cells glycosylation mutants for advancing glycobiology and biotechnology research.Scientific reports · 2024Article
- Enhanced N-Glycan Profiling of Therapeutic Monoclonal Antibodies through the Application of Upper-Hinge Middle-Up Level LC-HRMS Analysis.Antibodies (Basel, Switzerland) · 2024Article
- Characterization of a membrane Fcγ receptor in largemouth bass (Micropterus saloumoides) and its response to bacterial challenge.Fish physiology and biochemistry · 2024Article
- Assessment of monoclonal antibody glycosylation: a comparative study using HRMS, NMR, and HILIC-FLD.Analytical and bioanalytical chemistry · 2024Article
38 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Fc gamma receptor I (FcγRI) contributes to protective immunity against bacterial infections, but exacerbates certain autoimmune diseases. The sole high-affinity IgG receptor, FcγRI plays a significant role in immunotherapy. To elucidate the molecular mechanism of its high-affinity IgG binding, we determined the crystal structure of the extracellular domains of human FcγRI in complex with the Fc domain of human IgG1. FcγRI binds to the Fc in a similar mode as the low-affinity FcγRII and FcγRIII receptors. In addition to many conserved contacts, FcγRI forms additional hydrogen bonds and salt bridges with the lower hinge region of Fc. Unique to the high-affinity receptor-Fc complex, however, is the conformation of the receptor D2 domain FG loop, which enables a charged KHR motif to interact with proximal carbohydrate units of the Fc glycans. Both the length and the charge of the FcγRI FG loop are well conserved among mammalian species. Ala and Glu mutations of the FG loop KHR residues showed significant contributions of His-174 and Arg-175 to antibody binding, and the loss of the FG loop-glycan interaction resulted in an ∼ 20- to 30-fold decrease in FcγRI affinity to all three subclasses of IgGs. Furthermore, deglycosylation of IgG1 resulted in a 40-fold loss in FcγRI binding, demonstrating involvement of the receptor FG loop in glycan recognition. These results highlight a unique glycan recognition in FcγRI function and open potential therapeutic avenues based on antibody glycan engineering or small molecular glycan mimics to target FcγRI for certain 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.