Jiang Jiansheng, Natarajan Kannan, Margulies David H
Molecular Biology Section, Laboratory of Immune System Biology, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892, USA.
IUCrJ. 2024 May 1;11(Pt 3):287-298. doi: 10.1107/S2052252524002768.
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.
这项工作聚焦于由主要组织相容性复合体（MHC）编码的分子，这些分子结合自身、外来或肿瘤衍生的肽，并将其呈现在细胞表面以供T淋巴细胞（T细胞受体，TCR）和自然杀伤（NK）细胞上的受体识别。在过去几十年里，已经积累了关于MHC分子结构以及MHC/TCR与许多不同肽具有特异性的复合物的大量知识库。近年来，通过X射线晶体学和低温电子显微镜揭示了与协助肽加载的伴侣蛋白复合的MHC-I分子的结构。已使用诱变、分子动力学和核磁共振方法对这些结构进行了进一步研究。本综述总结了当前与抗原呈递过程相关的、控制肽交换的结构和动态原理。
