PDF(Pubmed)
Abstract：
This work focuses on molecules that are encoded by the major histocompatibility complex (MHC) and that bind self-, foreign- or tumor-derived peptides and display these at the cell surface for recognition by receptors on T lymphocytes (T cell receptors, TCR) and natural killer (NK) cells. The past few decades have accumulated a vast knowledge base of the structures of MHC molecules and the complexes of MHC/TCR with specificity for many different peptides. In recent years, the structures of MHC-I molecules complexed with chaperones that assist in peptide loading have been revealed by X-ray crystallography and cryogenic electron microscopy. These structures have been further studied using mutagenesis, molecular dynamics and NMR approaches. This review summarizes the current structures and dynamic principles that govern peptide exchange as these relate to the process of antigen presentation.
摘要：
这项工作的重点是由主要组织相容性复合体（MHC）编码并结合自身的分子，外来或肿瘤衍生的肽，并在细胞表面显示这些肽，以被T淋巴细胞上的受体识别（T细胞受体，TCR）和自然杀伤（NK）细胞。在过去的几十年中,已经积累了对许多不同肽具有特异性的MHC分子和MHC/TCR复合物的结构的大量知识基础。近年来,通过X射线晶体学和低温电子显微镜已经揭示了MHC-I分子与有助于肽负载的分子伴侣复合的结构。这些结构已使用诱变进一步研究，分子动力学和核磁共振方法。这篇综述总结了目前控制肽交换的结构和动力学原理，因为这些与抗原呈递过程有关。
