Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Antibody Structure01:10

Antibody Structure

67.6K
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...
67.6K
Antibody Structure01:10

Antibody Structure

15.2K
15.2K
Antibody Structure and Classes01:25

Antibody Structure and Classes

10.3K
Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
10.3K
Transcytosis of IgG01:15

Transcytosis of IgG

4.5K
Transcytosis is the process in which molecules are internalized by endocytosis, transported across the cell, and released through exocytosis from the opposite end of the cell. Molecules such as insulin, immunoglobulins, and certain nutrients are transferred through the recycling endosomes by recycling and transcytosis.
IgG molecules from a mother undergo transcytosis starting around 13 weeks of gestation. The amount of IgG transferred and entering the fetal blood circulation increases with...
4.5K
Structural Organization of the Human Body: An Overview01:18

Structural Organization of the Human Body: An Overview

37.5K
It is convenient to consider the body's structures in terms of fundamental levels of organization that increase in complexity: subatomic particles, atoms, molecules, organelles, cells, tissues, organs, organ systems, and organisms.
To study the chemical level of organization, scientists consider the simplest building blocks of matter: subatomic particles, atoms, and molecules. All matter in the universe is composed of one or more unique pure substances called elements, familiar examples of...
37.5K
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

4.6K
Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
4.6K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

From birds to man-Divergence and convergence in the co-evolution of an antibody/receptor complex.

Structure (London, England : 1993)·2026
Same author

Biophysical and functional characterization of IgE interactions with a malaria antigen.

Biochemical and biophysical research communications·2025
Same author

An Fc-Engineered Glycomodified Antibody Supports Proinflammatory Activation of Immune Effector Cells and Restricts Progression of Breast Cancer.

Cancer research·2025
Same author

Anti-IgD nanobodies as novel tools for studying human IgD biology.

Scientific reports·2025
Same author

Structure and activity of a phosphinothricin N-acetyltransferase (PSPTO_3321) from Pseudomonas syringae pv. tomato DC3000.

Biochemical and biophysical research communications·2025
Same author

The Crystal Structure of Human IgD-Fc Reveals Unexpected Differences With Other Antibody Isotypes.

Proteins·2024
Same journal

Diversity, Equality, and Inclusion in the naïve T Cell Receptor Repertoire.

Immunological reviews·2026
Same journal

Macrophage Plasticity and Immune Remodeling in Ischemic Heart Failure.

Immunological reviews·2026
Same journal

The T Cell Receptor: Molecular Sensor, Therapeutic Mediator and Probabilistic Driver of Adaptive Immunity.

Immunological reviews·2026
Same journal

Tissue-Resident Memory T Cells in the Heart: An Emerging Role in Chronic Inflammation.

Immunological reviews·2026
Same journal

Rethinking Immunity in Tissues: The Biology of Tertiary Lymphoid Structures.

Immunological reviews·2026
Same journal

Inflammation-Driven Lymphoid Structures: Organization, Function, and Clinical Impact Across Autoimmunity, Cancer, and Checkpoint Toxicity.

Immunological reviews·2026
See all related articles

Related Experiment Video

Updated: Mar 31, 2026

Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing
08:51

Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing

Published on: March 15, 2019

13.2K

Human IgG4: a structural perspective.

Anna M Davies1,2, Brian J Sutton1,2

  • 1Randall Division of Cell and Molecular Biophysics, King's College London, London, UK.

Immunological Reviews
|October 27, 2015
PubMed
Summary
This summary is machine-generated.

Human immunoglobulin G4 (IgG4) antibodies have unique properties, including limited effector functions beneficial for therapies. Recent crystal structures reveal unexpected IgG4-Fc conformations impacting Fcγ receptor interactions.

Keywords:
Fc receptorIgG1IgG4antibodyimmunoglobulin

More Related Videos

Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy
09:37

Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy

Published on: August 15, 2014

45.2K
Analysis of Somatic Hypermutation in the JH4 intron of Germinal Center B cells from Mouse Peyer's Patches
09:35

Analysis of Somatic Hypermutation in the JH4 intron of Germinal Center B cells from Mouse Peyer's Patches

Published on: April 20, 2021

7.4K

Related Experiment Videos

Last Updated: Mar 31, 2026

Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing
08:51

Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing

Published on: March 15, 2019

13.2K
Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy
09:37

Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy

Published on: August 15, 2014

45.2K
Analysis of Somatic Hypermutation in the JH4 intron of Germinal Center B cells from Mouse Peyer's Patches
09:35

Analysis of Somatic Hypermutation in the JH4 intron of Germinal Center B cells from Mouse Peyer's Patches

Published on: April 20, 2021

7.4K

Area of Science:

  • Immunology
  • Structural Biology
  • Biochemistry

Background:

  • Immunoglobulin G4 (IgG4) is the least abundant human IgG subclass, possessing unique biological characteristics like Fab-arm exchange and limited immune complex formation.
  • The reduced effector functions of IgG4, such as antibody-dependent cell-mediated cytotoxicity and complement-dependent cytotoxicity, make it a candidate for therapeutic applications.
  • IgG4 has a dual role in disease, acting protectively in allergies but detrimentally in malignant melanoma by hindering IgG1-mediated anti-tumor immunity.

Purpose of the Study:

  • To review the biological properties of human IgG4.
  • To discuss recent high-resolution crystal structures of IgG4-Fc.
  • To explore the implications of these structures for IgG4-Fcγ receptor interactions.

Main Methods:

  • Review of existing literature on IgG4 biology.
  • Analysis of recently published high-resolution crystal structures of IgG4-Fc.
  • Comparative analysis of IgG4-Fc structures with other IgG subclasses.

Main Results:

  • Recent crystal structures provide high-resolution insights into the IgG4-Fc conformation.
  • Unexpected conformations were observed in functionally significant Cγ2 domain loops of IgG4-Fc.
  • These structural findings offer new perspectives on IgG4 interactions with Fcγ receptors (FcγRs).

Conclusions:

  • Understanding IgG4's unique structural features, particularly in the Fc region, is crucial for elucidating its biological roles.
  • The observed conformational variations in IgG4-Fc may explain its distinct interactions with FcγRs compared to other IgG subclasses.
  • These insights are vital for harnessing IgG4's therapeutic potential and understanding its role in immune responses.