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单个T细胞受体如何识别自身和外来MHC

Leremy A Colf¹, Alexander J Bankovich, Nicole A Hanick

¹Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA.

|April 10, 2007

概括

T细胞受体 (TCR) 可以识别外来和自身蛋白质,这一过程称为全活性. 这项研究揭示了2C TCR使用不同的结构策略来结合不同的主要基因相容复合体 (MHC) 配体,挑战了TCR交叉反应中的分子模拟的想法.

科学领域:

免疫学免疫学免疫学
结构生物学结构生物学
生物化学生物化学

背景情况:

阿尔法贝塔T细胞受体 (TCRs) 与自身和外来主要基因相容性复合体 (MHC) 蛋白具有交叉反应性,这种现象被称为全活性.
了解 TCR 识别多种配体的结构基础对于免疫学和移植至关重要.

研究的目的:

阐明2C TCR与不同MHC-复合物的交叉活性背后的结构机制.
为了比较2C TCR如何与外来配体 (H-2L(d) -QL9) 与自身配体 (H-2K(b) -dEV8) 进行接触.

主要方法:

使用X射线晶体学来确定2C TCR的2.35A结构,该结构与H-2L(d) -QL9.9复合.
对2C TCR与外来 (H-2L(d) -QL9) 和自身 (H-2K(b) -dEV8) 连接物的比较结构分析.

主要成果:

2C TCR采用不同的结构策略来结合外来H-2L(d) -QL9和自身H-2K(b) -dEV8连接体.
对于每个连接体来说,TCR与MHC多态残留物和抗原进行了独特的双向接触.
在2C TCR和L(d) -QL9复合体之间观察到更大的结构互补性.
一种高亲和度的TCR变体保持了野生类型的结合方向,尽管TCR-CDR3α-相互作用发生了改变.

结论:

一个单一的TCR可以通过不同的结合机制来识别不同的配体,表明没有分子模拟的交叉反应性.
这些发现为T细胞受体全活性和带歧视的结构基础提供了新的见解.

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