ArticleNature communications2015
Structural basis for binding of human IgG1 to its high-affinity human receptor FcγRI.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 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.
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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
94 citing papers in PubMed.
- Equitable access to monoclonal antibodies targeting parasites.Trends in parasitology · 2026Review
- Structure-function analysis of the FCRL5-IgG1 Fc complex reveals an unappreciated pathway for B cell modulation by Fc-attenuated IgG.Science advances · 2026Article
- Mouse Fc-FcγRIV structure guides Fc engineering for cross-species FcγR recognition.bioRxiv : the preprint server for biology · 2026Article
- Hybrid Supercharged Antibodies: A Rational Approach to Boost Immunoassay Sensitivity via Controlled Nanoparticle Adsorption.Langmuir : the ACS journal of surfaces and colloids · 2026Article
- Structure-Function Analysis of the FCRL5-IgG1 Fc Complex Reveals an Unappreciated Effect of Fc-Silent Antibodies on B cells.bioRxiv : the preprint server for biology · 2026Article
- 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
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- IL-15 overexpression promotes memory program and anti-tumor activity of CD64 CAR T cells in a preclinical AML model.Communications biology · 2026Article
- Human FcRL5 is an Fc receptor that simultaneously engages two IgGs.Science advances · 2026Article
- Advancements and challenges in the management of chronic inducible urticaria.Frontiers in immunology · 2026Review
- Molecular mechanistic insights into the OX40-OX40L complex from biophysical and computational analyses.Protein science : a publication of the Protein Society · 2026Article
- Immunoglobulin germline reference sequences enable investigations and reveal insights into bat-specific immunity.iScience · 2025Article
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- Antigenic peptide delivery to antigen-presenting cells using a CD40-coiled coil affinity-based platform.Drug delivery · 2025Article
- Preclinical assessment of two FcγRI-specific antibodies that competitively inhibit immune complex-FcγRI binding to suppress autoimmune responses.Nature communications · 2025Article
- Cold Urticaria: From Wheals to Anaphylaxis.Allergy, asthma & immunology research · 2025Review
- Comprehensive Physico-Chemical and Functional Similarity Assessment of Intravenous and Subcutaneous RGB-19 Drug Products as Proposed Biosimilars to Tocilizumab Reference Product.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2025Article
- Exploring glycoform-dependent dynamic modulations in human immunoglobulin G via computational and experimental approaches.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
34 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cell-surface Fcγ receptors mediate innate and adaptive immune responses. Human Fcγ receptor I (hFcγRI) binds IgGs with high affinity and is the only Fcγ receptor that can effectively capture monomeric IgGs. However, the molecular basis of hFcγRI's interaction with Fc has not been determined, limiting our understanding of this major immune receptor. Here we report the crystal structure of a complex between hFcγRI and human Fc, at 1.80 Å resolution, revealing an unique hydrophobic pocket at the surface of hFcγRI perfectly suited for residue Leu235 of Fc, which explains the high affinity of this complex. Structural, kinetic and thermodynamic data demonstrate that the binding mechanism is governed by a combination of non-covalent interactions, bridging water molecules and the dynamic features of Fc. In addition, the hinge region of hFcγRI-bound Fc adopts a straight conformation, potentially orienting the Fab moiety. These findings will stimulate the development of novel therapeutic strategies involving hFcγRI.
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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.