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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...
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...
Antibody Structure and Classes01:25

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 Actions01:26

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...
Affinity and Avidity01:41

Affinity and Avidity

Overview
Antigens Involved in Adaptive Immunity01:26

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.

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Related Experiment Video

Updated: Jun 23, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

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

Published on: July 5, 2018

Structural basis of antibody-antigen interactions.

Eric J Sundberg1

  • 1Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA.

Methods in Molecular Biology (Clifton, N.J.)
|April 21, 2009
PubMed
Summary

Antibodies possess diverse structures enabling recognition of numerous antigens. This chapter explores antibody-antigen interactions, binding energetics, specificity, and affinity maturation.

Area of Science:

  • Immunology
  • Structural Biology
  • Protein Engineering

Background:

  • Antibodies are crucial for adaptive immunity, exhibiting vast structural diversity.
  • This diversity enables recognition of a nearly infinite array of antigens.
  • Understanding antibody structure-function relationships is key to immunology.

Purpose of the Study:

  • To elucidate the structural basis of antibody-antigen recognition.
  • To analyze the energetics and specificity of antibody-antigen binding.
  • To explore the role of conformational flexibility and affinity maturation in antibody function.

Main Methods:

  • Review of structural data and biophysical studies on antibody-antigen complexes.
  • Analysis of binding kinetics and thermodynamics.

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Using X-ray Crystallography, Biophysics, and Functional Assays to Determine the Mechanisms Governing T-cell Receptor Recognition of Cancer Antigens
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  • Examination of computational and experimental data on antibody flexibility.

    • Main Results:

    • Antibody structure provides a highly adaptable surface for antigen binding.
    • Binding energetics and specificity are governed by intricate molecular interactions.
    • Conformational flexibility plays a significant role in optimizing antigen recognition.
    • Affinity maturation involves structural changes that enhance binding.

    Conclusions:

    • Antibody structure and flexibility are critical for high-affinity, specific antigen recognition.
    • The principles governing antibody-antigen interactions have implications for therapeutic antibody design.
    • Further research into antibody structure-function is essential for advancing immunology and biotechnology.