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関連する概念動画

Antibody Structure01:10

Antibody Structure

65.2K
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...
65.2K
Cross-reactivity00:42

Cross-reactivity

32.8K
Overview
32.8K
Antibody Structure and Classes01:25

Antibody Structure and Classes

8.1K
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.
8.1K
Affinity and Avidity01:41

Affinity and Avidity

38.3K
Overview
38.3K
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.4K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.4K
Antibody Actions01:26

Antibody Actions

2.2K
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...
2.2K

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関連する実験動画

Updated: Jan 8, 2026

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
08:09

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Published on: March 24, 2017

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抗体-抗原構造における普遍的なパラトープ-エピトープ相互作用パターン

Marta A S Perez1,2, Vincent Zoete1,2

  • 1Ludwig Institute for Cancer Research, Lausanne Branch, Department of Oncology, Lausanne University Hospital (CHUV) and University of Lausanne (UNIL), Agora Cancer Research Center, Lausanne, Switzerland.

Protein science : a publication of the Protein Society
|December 23, 2025
PubMed
まとめ

研究者らは、抗体-抗原複合体構造を分析し、結合部位の重要なアミノ酸を特定した。この構造的洞察は、より優れた治療用抗体の開発と、抗体開発のための機械学習予測ツールの改善に役立つ。

キーワード:
抗体抗原エピトープ分子間相互作用パラトープ

さらに関連する動画

Synthetic Antigen Controls for Immunohistochemistry
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Synthetic Antigen Controls for Immunohistochemistry

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A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes
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A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes

Published on: March 25, 2014

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関連する実験動画

Last Updated: Jan 8, 2026

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
08:09

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Published on: March 24, 2017

9.9K
Synthetic Antigen Controls for Immunohistochemistry
09:30

Synthetic Antigen Controls for Immunohistochemistry

Published on: August 23, 2021

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A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes
07:59

A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes

Published on: March 25, 2014

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科学分野:

  • 構造生物学
  • 免疫学
  • 計算生物学

背景:

  • 抗体-抗原（Ab-Ag）相互作用は、免疫防御および治療用抗体開発にとって極めて重要である
  • これらの相互作用を構造レベルで予測および理解することは、効果的な治療法を設計するために不可欠である

研究 の 目的:

  • 抗体-抗原複合体の包括的な構造解析を実施する
  • パラトープ-エピトープ界面内の重要なアミノ酸（AA）とその位置を特定する
  • 抗体開発、特に機械学習での広範な利用のために相互作用パターンを標準化する

主な方法:

  • 抗体-抗原複合体の大規模で非冗長な3Dデータベースの広範な構造解析
  • 各相補性決定領域（CDR）位置のアミノ酸の検査
  • 同定されたパラトープ-エピトープ相互作用パターンの標準化

主要な成果:

  • CDR位置ごとのAA相互作用頻度が著しく異なることの実証
  • 相互作用データの標準化された形式の開発
  • 重要なアミノ酸とそのAb-Ag結合界面内の特定位置の同定

結論:

  • 本研究は、CDRループの標的化された洗練を通じて抗体結合を最適化するための重要な洞察を提供する
  • 本研究の結果は、より正確で信頼性の高いAb-Ag相互作用予測ツールの開発を支持する
  • 標準化されたデータは、治療用抗体設計における機械学習アプリケーションを容易にする