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Related Concept Videos

Antibody Structure01:10

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

G Protein–Coupled Receptors (GPCRs) are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to various stimuli. GPCRs regulate critical physiological pathways and are excellent drug targets for treating diseases such as diabetes, cancer, obesity, depression, or Alzheimer's. Nearly 35% of approved drugs implement their therapeutic effects by selectively interacting with specific GPCRs.
GPCRs are also called heptahelical, 7TM, or...

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Related Experiment Video

Updated: May 26, 2026

IP-FCM: Immunoprecipitation Detected by Flow Cytometry
12:17

IP-FCM: Immunoprecipitation Detected by Flow Cytometry

Published on: December 2, 2010

Mouse Fc-FcγRIV structure guides Fc engineering for cross-species FcγR recognition.

Yakendra Bajgain1, Mo Guo1, Kelli M Hager1

  • 1Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA.

Biorxiv : the Preprint Server for Biology
|May 25, 2026
PubMed
Summary

Understanding antibody Fc interactions with mouse Fc receptors (FcγRs) is crucial for predicting therapeutic antibody efficacy. This study reveals structural differences in Fc-FcγR binding, enabling engineering of antibodies for improved preclinical models and clinical translation.

Keywords:
Fc-FcγR interactionantibody engineeringantibody-dependent cellular cytotoxicitycrystal structureglycosylationmouse FcγRIVmouse IgG2a Fcrational Fc engineering

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Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells
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Last Updated: May 26, 2026

IP-FCM: Immunoprecipitation Detected by Flow Cytometry
12:17

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Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells
14:02

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells

Published on: April 9, 2018

Area of Science:

  • Immunology
  • Structural Biology
  • Biochemistry

Background:

  • Antibody-dependent cellular cytotoxicity (ADCC) is vital for therapeutic antibody function, mediated by Fc-FcγR interactions.
  • Current murine models have limited predictive value for human ADCC due to interspecies differences in Fc-FcγR binding.
  • Molecular details of mouse Fc-FcγR interactions are poorly understood, hindering clinical translation of preclinical data.

Purpose of the Study:

  • To elucidate the structural basis of mouse FcγRIV interactions with IgG Fc domains.
  • To understand species-specific differences in Fc-FcγR binding relevant to ADCC.
  • To engineer human Fc domains with improved cross-species FcγR recognition for better preclinical models.

Main Methods:

  • Determined the high-resolution crystal structure of mouse FcγRIV alone and complexed with mouse IgG2a Fc.
  • Compared structural features with the human IgG1 Fc-FcγRIIIa interface.
  • Utilized structure-guided design to create and test engineered human IgG1 Fc variants (Fc humo).

Main Results:

  • The mouse FcγRIV-IgG Fc structure shares similarities but also exhibits subtle variations compared to the human interface.
  • These variations, including receptor orientation and electrostatics, reduce human IgG1 Fc binding affinity to mouse FcγRIV.
  • Engineered Fc humo variant shows enhanced binding and activation of mouse FcγRIV while maintaining human FcγRIIIa engagement.

Conclusions:

  • Structural insights reveal species-specific constraints in Fc-FcγR interactions governing ADCC.
  • Engineering human Fc domains for cross-species FcγR recognition is feasible.
  • This approach offers a strategy to enhance the predictive power of preclinical models for therapeutic antibody development.