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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...

Antigens Involved in Adaptive Immunity

Antigens Involved in Adaptive Immunity

An antigen is any substance the immune system identifies as foreign and potentially harmful to the body, prompting an immune response. Antigens have two functional properties: immunogenicity and reactivity. Immunogenicity is the ability of an antigen to stimulate a specific immune response. At the same time, reactivity describes the antigen's ability to react with the cells and antibodies produced in response to it.
Complete Antigens
Complete antigens possess both immunogenicity and reactivity.

Antigen Processing Pathways

Antigen Processing Pathways

MHC molecules are key players in the immune response, enabling T cells to recognize and respond to specific antigens. They are present on the surface of all nucleated cells in the body and are instrumental in presenting antigens to T cells and activating them. T cells recognize the MHC-antigen complex and initiate an immune response. MHC class I and MHC class II are two main types of MHC molecules, each associated with a distinct antigen processing pathway.
MHC Class I: Presenting Endogenous...

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.

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: Jul 12, 2026

Using X-ray Crystallography, Biophysics, and Functional Assays to Determine the Mechanisms Governing T-cell Receptor Recognition of Cancer Antigens

Using X-ray Crystallography, Biophysics, and Functional Assays to Determine the Mechanisms Governing T-cell Receptor Recognition of Cancer Antigens

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The solution structure of a class II major histocompatibility complex superantigen binding domain

M J Jablonsky¹, P S Subramaniam, H M Johnson

¹Comprehensive Cancer Care Center, Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, 35294, USA.

Biochemical and Biophysical Research Communications

|May 29, 1997

Summary

Researchers determined the solution structure of a murine class II major histocompatibility (MHC) protein domain. This structure reveals how the domain binds to superantigens and peptides, offering insights into immune responses.

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Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β₂-Microglobulin

Published on: March 10, 2021

Area of Science:

Structural biology
Immunology
Biochemistry

Background:

Murine class II major histocompatibility (MHC) proteins play critical roles in the immune system.
Understanding the structure of MHC protein domains is essential for elucidating antigen presentation and immune recognition.
The specific domain I-Ab(beta)-(60-90) is known to interact with superantigens like staphylococcal enterotoxin A.

Purpose of the Study:

To determine the solution structure of the 31-residue I-Ab(beta)-(60-90) domain of a murine class II MHC protein.
To investigate the structural basis for the binding of this domain to superantigens.
To compare the structure of this murine MHC domain with homologous regions in human MHC proteins.

Main Methods:

Nuclear Magnetic Resonance (NMR) spectroscopy, specifically 600 MHz 1H NMR, was employed.
Distance geometry and dynamical simulated annealing calculations were utilized.
Constraints were derived from Nuclear Overhauser Effect Spectroscopy (NOESY) and Correlated Spectroscopy (COSY) experiments.

Main Results:

The solution structure of the I-Ab(beta)-(60-90) domain was determined, revealing it to be predominantly alpha-helical.
The structure showed greater similarity to the corresponding region in the human class II MHC protein HLA-DR1 than to the human class I MHC protein HLA-A2.
Specific residues, Arg-72, Arg-80, and His-81, were localized in relation to the peptide binding groove and the protein surface.

Conclusions:

The determined structure provides a molecular basis for understanding the interaction of the I-Ab(beta)-(60-90) domain with superantigens.
Histidine-81's position suggests a key role in binding both superantigens and antigenic peptides.
The structural similarity to HLA-DR1 highlights conserved features among class II MHC proteins.