Apostolopoulos V, Yu M, McKenzie I F, Wilson I A
Department of Molecular Biology and Skaggs Institute for Chemical Biology (BCC-206), Scripps Research Institute, 10550 N Torrey Pines Road, La Jolla, CA 92037, USA.
Curr Opin Mol Ther. 2000 Feb;2(1):29-36.
The major histocompatibility complex molecules bind and present short antigenic peptide fragments on the surface of antigen presenting cells to T-cell receptors. Recognition of peptide-MHC by cytotoxic T-cells initiates a cascade of signals to T-cells, which in turn destroy the antigen presenting cell. In the design of molecular vaccines for the treatment of diseases, an understanding of the 3-dimensional structure of MHC class I and is interaction with both peptide and T-cell receptor is an important prerequisite. In this review, we will discuss such crystal structures, as well as structures of glycopeptides and alternative T-cell antigens presented by MHC molecules.
主要组织相容性复合体分子在抗原呈递细胞表面结合并呈递短的抗原肽片段给T细胞受体。细胞毒性T细胞对肽-MHC的识别启动了一系列向T细胞传递的信号,进而破坏抗原呈递细胞。在设计用于治疗疾病的分子疫苗时,了解I类主要组织相容性复合体的三维结构及其与肽和T细胞受体的相互作用是一个重要的前提条件。在这篇综述中,我们将讨论此类晶体结构,以及糖肽的结构和由主要组织相容性复合体分子呈递的替代性T细胞抗原的结构。