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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 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.

Gene Families

Gene Families

Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...

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Related Experiment Video

Updated: Mar 7, 2026

Analysis of Histone Antibody Specificity with Peptide Microarrays

Analysis of Histone Antibody Specificity with Peptide Microarrays

Published on: August 1, 2017

Antibody H3 Structure Prediction.

C Marks¹, C M Deane¹

¹Department of Statistics, University of Oxford, 24-29 St Giles', Oxford OX1 3LB, United Kingdom.

Computational and Structural Biotechnology Journal

|February 24, 2017

Summary

This summary is machine-generated.

Accurately predicting the H3 loop structure in antibodies is crucial for drug development. This review covers computational methods for precise H3 loop structure prediction, enhancing antibody design.

Keywords:

Antibodies H3 Loop modelling Protein structure prediction

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Analysis of Histone Antibody Specificity with Peptide Microarrays

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Published on: August 1, 2017

Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy

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Published on: August 15, 2014

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:

Immunology
Structural Biology
Computational Chemistry

Background:

Antibodies are key immune proteins with diverse binding capabilities, making them valuable for therapeutics.
Antibody structure analysis aids rational drug design, but H3 loop prediction remains a challenge.
The H3 loop is critical for antibody-antigen binding and often difficult to determine experimentally or computationally.

Purpose of the Study:

To review and summarize existing computational approaches for predicting antibody H3 loop structures.
To highlight the importance of accurate H3 loop modeling in antibody engineering and drug development.

Main Methods:

Review of computational methodologies for H3 loop structure prediction.
Analysis of different algorithms and their performance in predicting H3 loop conformations.

Main Results:

Various computational strategies exist for H3 loop structure prediction, each with strengths and limitations.
The H3 loop's inherent flexibility and variability pose significant prediction challenges.

Conclusions:

Accurate computational H3 loop prediction is essential for advancing antibody-based therapeutics.
Further development of predictive models is needed to improve accuracy and reliability in antibody design.