Structural principles of MHC class II antigen presentation.
Structural principles of MHC class II antigen presentation.
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MHC II 类抗原呈递的结构原理。
DOI：
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发表时间：
1999
期刊：
影响因子：
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通讯作者：
D. Fremont
中科院分区：
文献类型：
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作者：
C. Nelson;D. Fremont
正常的免疫监视依赖于MHC II类分子结合肽抗原并将其携带到细胞表面以展示给T细胞的能力。为了有效地做到这一点，II类分子必须能够结合来自广泛的抗原序列的肽，并将它们保留在细胞表面足够长的时间，以使T细胞识别发生。II类分子通过巧妙的结构生物化学和至少两种不同分子伴侣的帮助的组合来完成这一任务：II类相关的不变链（Ii）;和非肽结合的II类分子，在小鼠中称为H2-DM，在人中称为HLA-DM（DM）。在这里，我们比较现有的3维结构的II类肽复合物，以审查肽结合和介绍的一般原则。我们将这种分析扩展到包括已知与MHC II类相互作用的蛋白质的结构，主要集中在Ii链和DM上。
Normal immune surveillance depends on the ability of MHC class II molecules to bind peptide antigens and carry them to the cell surface for display to T cells. To do this efficiently, class II molecules must be able to bind peptides from a broad array of antigen sequences and retain them at the cell surface long enough for T-cell recognition to occur. Class II molecules accomplish this task through a combination of clever structural biochemistry and the help of at least two different molecular chaperones: the class II-associated invariant chain (Ii); and a non-peptide binding class II molecule termed H2-DM in mouse and HLA-DM in man (DM). Here, we compare the existing 3-dimensional structures of class II-peptide complexes in order to review the general principles of peptide binding and presentation. We extend this analysis to include the structures of proteins known to interact with MHC class II, focusing primarily on the Ii chain and DM.