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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...

Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...

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-Protein Interfaces

Protein-Protein Interfaces

Protein Networks

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

Antibody Actions

Antibody Actions

Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...

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Related Experiment Video

Updated: Aug 27, 2025

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

Antibody interfaces revealed through structural mining.

Yizhou Yin¹, Matthew G Romei², Kannan Sankar²

¹Institute for Bioscience and Biotechnology Research and Department of Cell Biology and Molecular Genetics, University of Maryland College Park, College Park, MD, USA.

Computational and Structural Biotechnology Journal

|September 23, 2022

Summary

This summary is machine-generated.

Antibodies use weak, transient interactions to enhance function. Researchers discovered new antibody interfaces and validated their therapeutic potential through structural and functional studies.

Keywords:

Antibody Cluster Crystallography Homotypic Interface Oligomer Protein data bank Structure

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Last Updated: Aug 27, 2025

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Published on: July 5, 2018

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

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

Published on: March 15, 2019

Area of Science:

Immunology
Structural Biology
Biotherapeutics

Background:

Antibodies are crucial for humoral immunity and widely used as therapeutics.
Transient homotypic interactions are increasingly recognized as important for antibody function.
Investigating these weak interactions is challenging due to their transient nature.

Purpose of the Study:

To systematically characterize crystallographic interactions between antibody fragment antigen-binding (Fab) regions.
To discover and understand previously unrealized antibody interfaces.
To explore the potential of these interactions for antibody drug optimization.

Main Methods:

Comprehensive crystallographic analysis of antibody fragment antigen-binding (Fab) regions.
Identification of recurrent interaction motifs, including β-sheet and variable-constant elbow dimers.
Disulfide engineering to stabilize and experimentally validate identified interfaces.

Main Results:

Discovery of novel, previously unrecognized interfaces between antibody fragment antigen-binding (Fab) regions.
Identification of recurrent structural motifs, specifically β-sheet dimers and variable-constant elbow dimers.
Experimental validation of these interfaces through disulfide engineering, demonstrating structural and functional significance.

Conclusions:

This study provides the first comprehensive insight into undiscovered oligomeric interactions between antibodies.
The identified antibody interfaces offer new opportunities for the rational design and optimization of antibody-based therapeutics.
Understanding these interactions can enhance the development of more effective antibody drugs.