Rothbard J B
ImmuLogic Pharmaceutical Corporation, Palo Alto, CA 94304.
Semin Immunol. 1990 Sep;2(5):283-95.
The identification and sequencing of the antigen receptor of T cells coupled with the demonstration that MHC proteins specifically bind immunogenic peptides, and the solution of the crystal structure of HLA A2 and Aw68 collectively have led to a working model of how T cells recognize protein antigens. In contrast with many other known receptor-ligand interactions, this unique recognition mechanism has evolved to allow receptors on two separate cells to contact a common peptide ligand. To accomplish this, MHC proteins and the T cell receptor both differ from previously defined biological receptors in many respects. The MHC class I and II molecules are membrane glycoproteins that have evolved the remarkable capacity to bind and display on the surface of cells an extremely large number of structurally diverse peptides, while the antigen specific receptors of T cells are positively selected to specifically interact with the MHC protein alleles of the individual and only some of the repertoire of self peptides.
T细胞抗原受体的鉴定与测序，以及MHC蛋白特异性结合免疫原性肽的证明，还有HLA A2和Aw68晶体结构的解析，共同促成了一个关于T细胞如何识别蛋白质抗原的工作模型。与许多其他已知的受体-配体相互作用不同，这种独特的识别机制已经进化到允许两个不同细胞上的受体接触共同的肽配体。为了实现这一点，MHC蛋白和T细胞受体在许多方面都与先前定义的生物受体不同。MHC I类和II类分子是膜糖蛋白，它们进化出了非凡的能力，能够在细胞表面结合并展示大量结构多样的肽，而T细胞的抗原特异性受体经过阳性选择，以特异性地与个体的MHC蛋白等位基因以及部分自身肽库相互作用。
