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Antibody Structure

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...

Antibody Structure

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...

Antibody Structure and Classes

Antibody Structure and Classes

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.

Protein and Protein Structure

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...

Transcytosis of IgG

Transcytosis of IgG

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...

Protein Modifications in the RER

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.

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Related Experiment Video

Updated: Jul 6, 2026

Double Labeling Immunofluorescence using Antibodies from the Same Species to Study Host-Pathogen Interactions

Double Labeling Immunofluorescence using Antibodies from the Same Species to Study Host-Pathogen Interactions

Published on: July 10, 2021

Human IgG2 antibodies display disulfide-mediated structural isoforms.

Jette Wypych¹, Ming Li, Amy Guo

¹Department of Analytical Sciences, Amgen Inc., Thousand Oaks, California 91320, USA. jwypych@amgen.com

The Journal of Biological Chemistry

|March 15, 2008

Summary

Human immunoglobulin G2 (IgG2) molecules exhibit previously undiscovered structural diversity. Analysis reveals three distinct covalent structures (IgG2-A, -B, and -A/B) due to novel disulfide bonding patterns in antibodies.

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

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Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

Area of Science:

Immunology
Structural Biology
Biochemistry

Background:

Human immunoglobulin G2 (IgG2) is a crucial antibody subclass.
The established covalent structure of IgG2 has been widely accepted.
Previous studies have not fully characterized the disulfide bond heterogeneity in IgG2.

Purpose of the Study:

To investigate the covalent structure of human IgG2 molecules.
To identify and characterize novel structural isoforms of human IgG2.
To understand the implications of disulfide bond variations in IgG2 structure.

Main Methods:

Detailed analysis of recombinant human IgG2 monoclonal antibody.
Characterization of disulfide bond structures.
Comparison of novel structures with existing literature.

Main Results:

Human IgG2 antibodies can be resolved into distinct structural forms based on disulfide bonds.
Three main structural types were identified: IgG2-A (classic), IgG2-B (symmetrical complex), and IgG2-A/B (intermediate).
Novel isoforms involve covalent linkages between light chain constant domain, heavy chain C(H)1 domain, and the hinge region.

Conclusions:

Disulfide structural heterogeneity is a natural feature of human IgG2 subclass.
These novel isoforms are present in native IgG2 from myeloma plasma and normal serum.
The structural variations occur with both kappa and lambda light chains, albeit with differing ratios.