Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Antibody Structure

Antibody Structure

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 Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

Ligand Binding and Linkage

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...

You might also read

Related Articles

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

Sort by

Same author

Impaired collagen deposition in the absence of ERp44.

iScience·2026

Same author

A regulatory circuit operated by KDELR1 and KDELR3 fine-tunes the composition of the early secretory pathway.

Cellular and molecular life sciences : CMLS·2026

Same author

Mitochondria remodeling during endometrial stromal cell decidualization.

Life science alliance·2024

Same author

Congress of multiple dimers is needed for cross-phosphorylation of IRE1α and its RNase activity.

Life science alliance·2024

Same author

Erratum: A tetracationic porphyrin with dual anti-prion activity.

iScience·2023

Same author

Correction: Time- and cost-effective production of untagged recombinant MVA by flow virometry and direct virus sorting.

Journal of translational medicine·2023

Search research articles

Related Experiment Video

Updated: May 3, 2026

Detection of Heterodimerization of Protein Isoforms Using an in Situ Proximity Ligation Assay

Detection of Heterodimerization of Protein Isoforms Using an in Situ Proximity Ligation Assay

Published on: October 20, 2018

Missing links in antibody assembly control.

Tiziana Anelli¹, Eelco van Anken¹

¹Division of Genetics and Cell Biology, San Raffaele Scientific Institute, Via Olgettina 60, 20132 Milan, Italy.

International Journal of Cell Biology

|February 4, 2014

Summary

This summary is machine-generated.

Quiescent B cells use thiol-mediated retention to prevent premature antibody secretion. ERp44 controls this process, which is overridden in activated B cells by pERp1/MZB1 for antibody release.

More Related Videos

Analysis of Protein-protein Interactions and Co-localization Between Components of Gap, Tight, and Adherens Junctions in Murine Mammary Glands

Analysis of Protein-protein Interactions and Co-localization Between Components of Gap, Tight, and Adherens Junctions in Murine Mammary Glands

Published on: May 30, 2017

Semi-automated Biopanning of Bacterial Display Libraries for Peptide Affinity Reagent Discovery and Analysis of Resulting Isolates

Semi-automated Biopanning of Bacterial Display Libraries for Peptide Affinity Reagent Discovery and Analysis of Resulting Isolates

Published on: December 6, 2017

Related Experiment Videos

Last Updated: May 3, 2026

Detection of Heterodimerization of Protein Isoforms Using an in Situ Proximity Ligation Assay

Detection of Heterodimerization of Protein Isoforms Using an in Situ Proximity Ligation Assay

Published on: October 20, 2018

Analysis of Protein-protein Interactions and Co-localization Between Components of Gap, Tight, and Adherens Junctions in Murine Mammary Glands

Analysis of Protein-protein Interactions and Co-localization Between Components of Gap, Tight, and Adherens Junctions in Murine Mammary Glands

Published on: May 30, 2017

Semi-automated Biopanning of Bacterial Display Libraries for Peptide Affinity Reagent Discovery and Analysis of Resulting Isolates

Semi-automated Biopanning of Bacterial Display Libraries for Peptide Affinity Reagent Discovery and Analysis of Resulting Isolates

Published on: December 6, 2017

Area of Science:

Immunology
Cell Biology
Biochemistry

Background:

B lymphocytes must control immunoglobulin M (IgM) secretion for humoral immune response fidelity.
Membrane-bound IgM functions as the B cell receptor for antigen recognition.
Secretory IgM requires specific assembly for proper function and secretion.

Purpose of the Study:

To discuss recent findings on ERp44's role in IgM assembly control.
To explore the pH-dependent mechanism of thiol-mediated retention by ERp44.
To investigate the potential role of pERp1/MZB1 in overriding IgM retention.

Main Methods:

Discussion of recent findings on protein disulfide isomerase family members.
Analysis of pH-dependent interactions in the endoplasmic reticulum and cis-Golgi.
Exploration of co-chaperone interactions with GRP94.

Main Results:

ERp44 mediates thiol-mediated retention of unassembled secretory IgM subunits.
ERp44's retention activity is pH-dependent and involves shuttling between cellular compartments.
pERp1/MZB1 may facilitate the release of IgM from ERp44-mediated retention in activated B cells.

Conclusions:

ERp44 acts as a critical quality control checkpoint for IgM assembly via thiol-mediated retention.
pH regulation and specific co-chaperones are key to controlling antibody secretion.
Understanding these mechanisms is vital for regulating humoral immune responses.