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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.

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Related Experiment Video

Updated: May 5, 2026

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

Antibody variable domain interface and framework sequence requirements for stability and function by high-throughput

Hung-Ju Hsu¹, Kuo Hao Lee², Jhih-Wei Jian³

¹Graduate Institute of Life Sciences, National Defense Medical Center, Taipei 114, Taiwan; Genomics Research Center, Academia Sinica, Taipei 115, Taiwan.

Structure (London, England : 1993)

|November 26, 2013

Summary

This summary is machine-generated.

Protein core stability is flexible and indirectly impacts antigen binding. Interdomain interfaces directly influence antigen binding, suggesting they are part of the binding site.

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Area of Science:

Protein engineering
Structural biology
Immunology

Background:

Protein structure, stability, and function depend on intradomain cores and interdomain interfaces.
Elucidating sequence-structure-function relationships in protein packing is challenging due to combinatorial complexity.

Purpose of the Study:

To investigate the sequence preferences and functional roles of residues in protein cores and interfaces.
To understand how protein structural elements relate to antigen binding and stability.

Main Methods:

Randomizing beta strand residues in model antibody variable domains using saturated mutagenesis.
Selecting functional variants via high-throughput sequencing.
Measuring thermal stability of variants using high-throughput methods.

Main Results:

Intradomain hydrophobic core residues exhibit flexible sequence preferences, indirectly stabilizing protein structure and antigen binding.
Interdomain interface residues show direct coupling with antigen binding.
Antibody variable domains demonstrate distinct roles for core and interface residues.

Conclusions:

The interdomain interface is functionally integral to the antigen-binding site.
Protein core stability is achieved through flexible residue choices, indirectly affecting function.
Understanding these relationships aids in protein design and engineering.