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Protein Folding01:22

Protein Folding

Overview
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...
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 Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Structure of Cadherins01:25

Structure of Cadherins

The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...
Complement System01:27

Complement System

The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a membrane...

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関連する実験動画

Updated: Jul 15, 2026

Measuring the 50% Haemolytic Complement (CH50) Activity of Serum
08:26

Measuring the 50% Haemolytic Complement (CH50) Activity of Serum

Published on: March 29, 2010

C3bの構造は,補完活動の基礎となる形状の変化を明らかにします.

Bert J C Janssen1, Agni Christodoulidou, Andrew McCarthy

  • 1Crystal and Structural Chemistry, Bijvoet Center for Biomolecular Research, Faculty of Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.

Nature
|October 20, 2006
PubMed
まとめ

コンプリメント・システムは,補足システムです.

科学分野:

  • 免疫学 免疫学とは
  • 構造生物学 構造生物学とは
  • バイオケミストリー バイオケミストリー

背景:

  • 補完系は,先天性および適応性免疫に不可欠であり,感染抵抗と細胞残骸の除去に役立ちます.
  • 活性補完タンパク質3 (C3b) は,表面に共性的に結合し,免疫反応を増幅し,細胞をファゴサイトーシスにマークします.
  • C3のC3bへの形状の変化は,その結合部位を暴露し,大部分は未知のままである.

研究 の 目的:

  • 補完タンパク質3 (C3) のC3bへのプロテオリチス活性化に伴う構造変化を解明する.
  • 活性化されたC3bの結晶構造と詳細なドメインの再編成を提示する.
  • C3bがタンパク質と受容体の相互作用のための結合部位をどのように露出させるかを理解する.

主な方法:

  • 4-Å解像度で活性補完タンパク質C3bの結晶構造を決定しました.
  • タンパク質分解活性化時にC3bの12ドメインの構成的再配置を分析した.
  • 主な変化を特定するために,活性化されたC3bとネイティブC3の構造を比較しました.

主要な成果:

  • 結晶構造は,C3bのC3.3と比べて,C3bのドメインの重要な再編成を明らかにしています.

さらに関連する動画

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment
07:26

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment

Published on: July 18, 2017

Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion
06:54

Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion

Published on: June 15, 2019

関連する実験動画

Last Updated: Jul 15, 2026

Measuring the 50% Haemolytic Complement (CH50) Activity of Serum
08:26

Measuring the 50% Haemolytic Complement (CH50) Activity of Serum

Published on: March 29, 2010

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment
07:26

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment

Published on: July 18, 2017

Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion
06:54

Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion

Published on: June 15, 2019

  • C3bのチオエステル部位は,共振結合に完全に露出しており,C3.3の埋もれた位置から著しく変化しています.
  • 変異した分子表面は,因子Bと補完レギュレータの結合部位と一致する神秘的な部位を暴露します.

    • 結論:

    • C3からC3bへのプロテオリスティック活性化には,主に初期変換段階における主要な形状の変化が含まれます.
    • C3bの形成に関するこれらの構造的な洞察は,その機能的結合部位がどのように露出されているかを明らかにします.
    • これらの構造的ダイナミクスを理解することは,補足媒介性炎症障害の治療戦略の開発に不可欠です.