Major Histocompatibility Complex class I (MHC I) molecules are highly polymorphic, with allotypes differing in peptide binding preferences, and in their dependence upon tapasin for optimal peptide selection. The tapasin dependence of MHC allotypes is inversely correlated with their self-editing ability, and underpinned by conformational plasticity. Recently, TAPBPR has been shown to enhance MHC I assembly via a chaperone-like function, and by editing the peptide repertoire of some MHC I allotypes. Structural analysis has shown TAPBPR binding changes the conformation and dynamics of MHC I, with MHC protein dynamics likely to determine the prevailing TAPBPR function: generically enhancing MHC I assembly by stabilising highly dynamic peptide-empty MHC I; and by editing the peptide repertoire of highly dynamic MHC I allotypes.

中文翻译：

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MHC I 蛋白动力学在 Tapasin 和 TAPBPR 辅助免疫肽组编辑中的作用。

主要组织相容性复合物 I 类 (MHC I) 分子具有高度多态性，其同种异型在肽结合偏好方面不同，并且它们依赖于 Tapasin 以进行最佳肽选择。MHC 同种异型的tapasin 依赖性与其自我编辑能力成反比，并以构象可塑性为基础。最近，TAPBPR 已被证明可通过类似伴侣的功能和编辑某些 MHC I 同种异型的肽库来增强 MHC I 组装。结构分析表明 TAPBPR 结合改变了 MHC I 的构象和动力学，MHC 蛋白动力学可能决定主要的 TAPBPR 功能：通过稳定高度动态的肽空 MHC I 一般增强 MHC I 组装；并通过编辑高度动态的 MHC I 同种异型的肽库。