Structural aspects of chaperone-mediated peptide loading in the MHC-I antigen presentation pathway.
Structural aspects of chaperone-mediated peptide loading in the MHC-I antigen presentation pathway.
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MHC-I 抗原呈递途径中伴侣介导的肽加载的结构方面。
DOI：
10.1080/10409238.2019.1610352
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发表时间：
2019
影响因子：
6.5
通讯作者：
Margulies,DavidH
中科院分区：
文献类型：
--
作者：
Natarajan,Kannan;Jiang,Jiansheng;Margulies,DavidH
细胞先天性和适应性免疫系统对外来和失调抗原的识别在很大程度上取决于肽/MHC (pMHC) 复合物的细胞表面展示。这种复合物的形成需要抗原肽的产生、MHC分子的正确折叠、将肽装载到MHC分子上、糖基化以及转运到质膜。这一系列复杂的生物合成、生化和细胞生物反应被称为“抗原加工和呈递”。在这里，我们总结了最近的工作，重点关注关键 MHC-I 专用伴侣、tapasin 和 TAPBPR 的结构和功能表征。这些机制反映了构象柔性分子适应其配体的能力，并且与 MHC-II 途径中肽抗原加载所利用的类似过程相当。
Recognition of foreign and dysregulated antigens by the cellular innate and adaptive immune systems is in large part dependent on the cell surface display of peptide/MHC (pMHC) complexes. The formation of such complexes requires the generation of antigenic peptides, proper folding of MHC molecules, loading of peptides onto MHC molecules, glycosylation, and transport to the plasma membrane. This complex series of biosynthetic, biochemical, and cell biological reactions is known as “antigen processing and presentation”. Here, we summarize recent work, focused on the structural and functional characterization of the key MHC-I-dedicated chaperones, tapasin, and TAPBPR. The mechanisms reflect the ability of conformationally flexible molecules to adapt to their ligands, and are comparable to similar processes that are exploited in peptide antigen loading in the MHC-II pathway.