Structure and Function of Molecular Chaperones that Govern Immune Peptide Loading.
Structure and Function of Molecular Chaperones that Govern Immune Peptide Loading.
复制标题
控制免疫肽加载的分子伴侣的结构和功能。
DOI：
10.1007/978-3-030-28151-9_10
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发表时间：
2019
影响因子：
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通讯作者：
Natarajan,Kannan
中科院分区：
文献类型：
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作者：
Margulies,DavidH;Jiang,Jiansheng;Natarajan,Kannan
Major histocompatibility class I (MHC-I) molecules bind peptides derived from cellular synthesis and display them at the cell surface for recognition by receptors on T lymphocytes (TCR) or natural killer (NK) cells. Such recognition provides a crucial step in autoimmunity, identification of bacterial and viral pathogens, and anti-tumor responses. Understanding the mechanism by which such antigenic peptides in the ER are loaded and exchanged for higher affinity peptides onto MHC molecules has recently been clarified by cryo-EM and X-ray studies of the multimolecular peptide loading complex (PLC) and a unimolecular tapasin-like chaperone designated TAPBPR. Insights from these structural studies and complementary solution NMR experiments provide a basis for understanding mechanisms related to immune antigen presentation.
