Engelhard V H
Department of Microbiology, University of Virginia, Charlottesville 22908.
Annu Rev Immunol. 1994;12:181-207. doi: 10.1146/annurev.iy.12.040194.001145.
Class I and class II molecules encoded by genes within the major histocompatibility complex play a central role in regulation of immune responses through their ability to bind and display small peptides derived from foreign antigens. Within the last few years, considerable progress has been made in understanding the structures of class I and class II MHC molecules, as well as the features of the peptides that are their principal ligands. This review summarizes this information and describes how it accounts for both the specificity and degeneracy of peptide binding. It also considers how the origin and structural features of peptides that have been isolated from MHC molecules, so-called "naturally processed" peptides, have provided insight into the pathways through which the peptides are produced. Finally, the use of new structural information and techniques for peptide characterization for the identification of peptides that comprise epitopes for individual antigen-specific T cells are considered.
主要组织相容性复合体中的基因所编码的I类和II类分子，通过其结合并呈递源自外来抗原的小肽的能力，在免疫反应调节中发挥核心作用。在过去几年里，在了解I类和II类MHC分子的结构以及作为其主要配体的肽的特征方面取得了相当大的进展。本综述总结了这些信息，并描述了其如何解释肽结合的特异性和简并性。它还考虑了从MHC分子中分离出的肽（即所谓的“天然加工”肽）的起源和结构特征如何为肽的产生途径提供了见解。最后，探讨了如何利用新的结构信息和肽表征技术来鉴定构成个体抗原特异性T细胞表位的肽。
