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首页> 外文期刊>Annual review of cell and developmental biology >Regulation of MHC class I assembly and peptide binding
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Regulation of MHC class I assembly and peptide binding

机译:调节MHC I类装配和肽结合

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Peptide binding to MHC class I molecules is a component of a folding and assembly process that occurs in the endoplasmic reticulum (ER) and uses both cellular chaperones and dedicated factors. The involvement of glycoprotein quality-control chaperones and cellular oxidoreductases in peptide binding has led to models that are gradually being refined. Some aspects of the peptide loading process (e.g., the biosynthesis and degradation of MHC class I complexes) conform to models of glycoprotein quality control, but other aspects (e.g., the formation of a stable disulfide-linked dimer between tapasin and ERp57) deviate from models of chaperone and oxidoreductase function. Here we review what is known about the intersection of glycoprotein folding, oxidative reactions, and MHC class I peptide loading, emphasizing events that occur in the ER and within the MHC class I peptide loading complex.
机译:与I类MHC分子结合的肽是内质网(ER)中发生的折叠和组装过程的组成部分,并且同时使用细胞伴侣和专用因子。糖蛋白质量控制伴侣和细胞氧化还原酶参与肽结合已导致模型逐渐完善。肽加载过程的某些方面(例如,MHC I类复合物的生物合成和降解)符合糖蛋白质量控制模型,但其他方面(例如,在塔帕胶和ERp57之间形成稳定的二硫键连接的二聚体)与伴侣和氧化还原酶功能的模型。在这里,我们回顾了有关糖蛋白折叠,氧化反应和MHC I类肽负载的交叉点的已知信息,重点介绍了在ER和MHC I类肽负载复合物中发生的事件。

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