Department of Pathology, University of Cambridge, Cambridge CB2 1QP , UK.
Department of Pathology, University of Cambridge, Cambridge CB2 1QP , UK.
Curr Opin Immunol. 2023 Aug;83:102346. doi: 10.1016/j.coi.2023.102346. Epub 2023 Jun 7.
Since the discovery of Transporter associated with antigen processing-binding protein-related (TAPBPR) over two decades ago, extensive studies have explored its function in the context of the major histocompatibility complex class-I (MHC-I) antigen processing and presentation pathway. As a chaperone and peptide editor, TAPBPR was recently revealed to have overlapping structural features when resolved with peptide-receptive MHC-I molecules compared with the two newly solved tapasin:MHC-I structures. Despite this, the two chaperones seem to have a unique criteria for loading high-affinity peptides on MHC-I molecules. Yet, the mechanism of action of how TAPBPR creates its distinct filter in cargo selection for peptide-receptive MHC-I molecules continues to be a subject of debate.
自二十多年前发现与抗原加工结合蛋白相关的转运蛋白(TAPBPR)以来,大量研究已经探索了其在主要组织相容性复合体 I 类(MHC-I)抗原加工和呈递途径中的功能。作为伴侣蛋白和肽编辑物,TAPBPR 最近在与肽接受性 MHC-I 分子解析时显示出与新解决的 tapasin:MHC-I 结构重叠的结构特征。尽管如此,这两种伴侣蛋白似乎具有独特的标准,用于将高亲和力的肽加载到 MHC-I 分子上。然而,TAPBPR 如何为肽接受性 MHC-I 分子创造其独特的货物选择过滤器的作用机制仍然是一个争论的话题。