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Updated: Jun 10, 2026

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Expansion of Human Peripheral Blood γδ T Cells using Zoledronate
Published on: September 9, 2011
人間のガンマデルタT細胞抗原受容体の構造
T J Allison1, C C Winter, J J Fournié
1Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, Rockville, Maryland 20852, USA. tallison@niaid.nih.gov
Nature
|July 19, 2001
まとめ
この研究は,ガンマデルタT細胞受容体 (ガンマデルタTCR) のユニークな構造を明らかにし,彼らがどのようにフォスフォアンチゲンを認識するのかを説明しています. これらの発見は,ガンマデルタTCRの機能と,アルファベータTCRと比較して異なるシグナリング複合体についての洞察を提供します.
科学分野:
- 免疫学 免疫学とは
- 構造生物学 構造生物学とは
- 分子生物学は分子生物学である.
背景:
- ガンマデルタT細胞受容体 (ガンデルタTCR) は,アルファベータTCRとは異なり,無傷のタンパク質や非ペプチド化合物を認識する.
- 周辺血液T細胞の約5%がガンマデルタTCRを発現し,主に非ペプチドリン酸化抗原を認識する.
- ガンマデルタのTCR構造を理解することは,それらのユニークな抗原認識機構の解明に不可欠です.
研究 の 目的:
- ヒトのフォスフォアンチゲン反応性ガンマデルタ TCR.の高解像度構造を決定する.
- ガンマデルタTCRの構造特性をアルファベタTCRと抗体と比較する.
- 特定のガンマデルタ TCR 遺伝子セグメントによるフォスフォアンチゲンの認識のための構造的基礎を提供すること.
主な方法:
- X線結晶学を使用して,人間のガンマデルタTCRの構造を3.1 Å解像度で決定しました.
- ガンマデルタTCR,アルファベタTCR,および抗体間の比較構造分析が行われました.
- 互補性を決定する地域 (CDR) とドメイン指向の分析が行われました.
主要な成果:
- 変数 (V) と定数 (C) の領域のユニークな方向性は,VgammaとCgammaドメインの間の小さな角度から生じるガンマデルタTCRで観察されました.
- VドメインのCDRは,リン酸化抗原のための化学的に妥当な結合部位を示し,Vgamma9とVdelta2の遺伝子セグメントの使用を説明します.
- アルファベータTCRと比較して,Cドメイン (CgammaとCdelta) とその鎖間ジスルフィード結合において,重要な構造的差異が認められた.
結論:
- 決定された構造は,ガンマデルタTCRsによるフォスフォアンチゲン認識の分子説明を提供します.
- ガンマデルタTCR Cドメインの独特の構造的特徴は,アルファベタTCRとは異なる認識/シグナリング複合体を形成することを示唆しています.
- この構造的洞察は,T細胞受容体の多様性や免疫認識経路についての理解を深める.
関連する概念動画
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The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
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
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...
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...
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Naive T cells that have not yet encountered an antigen express two primary CD...
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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.
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.

