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

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 and Protein Structure02:15

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...
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...
Globular Proteins01:27

Globular Proteins

In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...
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...

You might also read

Related Articles

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

Sort by
Same author

Absent the pre-B cell receptor checkpoint, the B-1a immunoglobulin CDR-H3 repertoire normalizes by convergent selection.

Frontiers in immunology·2026
Same author

A type-specific B-cell epitope at the apex of outer surface protein C (OspC) of the Lyme disease spirochete, <i>Borreliella burgdorferi</i>.

Microbiology spectrum·2025
Same author

The SNMMI Procedure Standard/ACNM Practice Guideline for Gastrointestinal Bleeding Scintigraphy 3.0.

Journal of nuclear medicine technology·2025
Same author

Fc-engineered antibodies promote neutrophil-dependent control of Mycobacterium tuberculosis.

Nature microbiology·2024
Same author

Discordant Phenotypes of Nephritis in Patients with X-linked Agammaglobulinemia.

Journal of clinical immunology·2024
Same author

Single-domain antibodies reveal unique borrelicidal epitopes on the Lyme disease vaccine antigen, outer surface protein A (OspA).

Infection and immunity·2024
Same journal

Corrigendum.

The Journal of allergy and clinical immunology·2026
Same journal

Comparative Efficacy of Biologic Agents for Severe Chronic Rhinosinusitis with Nasal Polyps: A Systematic Review and Network Meta-analysis.

The Journal of allergy and clinical immunology·2026
Same journal

Tamoxifen-driven neutrophil reprogramming protects from pulmonary Granulibacter bethesdensis infection in chronic granulomatous disease.

The Journal of allergy and clinical immunology·2026
Same journal

Clinical and transcriptomic characterization of mixed granulocytic COPD phenotype.

The Journal of allergy and clinical immunology·2026
Same journal

Dupilumab outcomes in pediatric asthma by early eosinophil status: post hoc analysis of VOYAGE/EXCURSION.

The Journal of allergy and clinical immunology·2026
Same journal

Maternal antibiotic exposure alters the newborn metabolomic profile and increases the risk of respiratory infections in offspring: a 13-year longitudinal birth cohort study.

The Journal of allergy and clinical immunology·2026
See all related articles

Related Experiment Video

Updated: May 7, 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

Structure and function of immunoglobulins.

Harry W Schroeder1, Lisa Cavacini

  • 1Division of Clinical Immunology and Rheumatology, Department of Medicine, University of Alabama at Birmingham, Birmingham, AL 35294-2182, USA. hwsj@uab.edu

The Journal of Allergy and Clinical Immunology
|February 24, 2010
PubMed
Summary
This summary is machine-generated.

Immunoglobulins, or antibodies, are proteins with variable regions for antigen binding and constant regions for effector functions. Their structure allows for diverse immune responses and targeted therapies.

More Related Videos

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

Double Labeling Immunofluorescence using Antibodies from the Same Species to Study Host-Pathogen Interactions
07:35

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

Published on: July 10, 2021

Related Experiment Videos

Last Updated: May 7, 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

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

Double Labeling Immunofluorescence using Antibodies from the Same Species to Study Host-Pathogen Interactions
07:35

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

Published on: July 10, 2021

Area of Science:

  • Immunology
  • Molecular Biology
  • Protein Chemistry

Background:

  • Immunoglobulins (antibodies) are crucial immune proteins.
  • They consist of two heavy and two light chains, forming distinct functional domains.

Purpose of the Study:

  • To detail the structural and functional organization of immunoglobulins.
  • To explain the mechanisms underlying antibody diversity and effector functions.

Main Methods:

  • Analysis of immunoglobulin protein structure and function.
  • Review of genetic mechanisms (gene rearrangement, somatic hypermutation) shaping antibody variability.
  • Classification of immunoglobulin isotypes and subclasses.

Main Results:

  • Variable domains, formed by complementarity-determining regions (CDRs), mediate antigen binding.
  • Constant domains dictate effector functions (e.g., complement activation, Fc receptor binding).
  • Gene rearrangement and somatic hypermutation generate diverse antigen-binding specificities and affinities.
  • Five main isotypes (IgM, IgG, IgA, IgD, IgE) and subclasses (IgG1-4, IgA1-2) exhibit distinct biological properties.

Conclusions:

  • Immunoglobulin structure is intricately linked to its diverse immune functions.
  • The modular nature of immunoglobulins allows for adaptation and specificity in immune responses.