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T 细胞受体的结构生物学:受体组装、配体识别和信号起始的见解。

Structural biology of the T-cell receptor: insights into receptor assembly, ligand recognition, and initiation of signaling.

机构信息

Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Boston, Massachusetts 02115, USA.

出版信息

Cold Spring Harb Perspect Biol. 2010 Apr;2(4):a005140. doi: 10.1101/cshperspect.a005140. Epub 2010 Mar 17.

DOI:10.1101/cshperspect.a005140
PMID:20452950
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2845206/
Abstract

The T-cell receptor (TCR)-CD3 complex serves as a central paradigm for general principles of receptor assembly, ligand recognition, and signaling in the immune system. There is no other receptor system that matches the diversity of both receptor and ligand components. The recent expansion of the immunological structural database is beginning to identify key principles of MHC and peptide recognition. The multicomponent assembly of the TCR complex illustrates general principles used by many receptors in the immune system, which rely on basic and acidic transmembrane residues to guide assembly. The intrinsic binding of the cytoplasmic domains of the CD3epsilon and zeta chains to the inner leaflet of the plasma membrane represents a novel mechanism for control of receptor activation: Insertion of critical CD3epsilon tyrosines into the hydrophobic membrane core prevents their phosphorylation before receptor engagement.

摘要

T 细胞受体 (TCR)-CD3 复合物是免疫受体组装、配体识别和信号转导的一般原则的典范。没有其他受体系统能够与受体和配体成分的多样性相匹配。免疫结构数据库的最新扩展开始确定 MHC 和肽识别的关键原则。TCR 复合物的多组分组装说明了免疫系统中许多受体所使用的一般原则,这些原则依赖于碱性和酸性跨膜残基来指导组装。CD3epsilon 和 zeta 链的细胞质结构域与质膜内叶的固有结合代表了一种控制受体激活的新机制:将关键的 CD3epsilon 酪氨酸插入疏水性膜核心中,可防止受体结合前的磷酸化。

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