• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >The structure and stability of the monomorphic HLA-G are influenced by the nature of the bound peptide.
【24h】

The structure and stability of the monomorphic HLA-G are influenced by the nature of the bound peptide.

机译：单态HLA-G的结构和稳定性受结合肽的性质影响。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The highly polymorphic major histocompatibility complex class Ia (MHC-Ia) molecules present a broad array of peptides to the clonotypically diverse alphabeta T-cell receptors. In contrast, MHC-Ib molecules exhibit limited polymorphism and bind a more restricted peptide repertoire, in keeping with their major role in innate immunity. Nevertheless, some MHC-Ib molecules do play a role in adaptive immunity. While human leukocyte antigen E (HLA-E), the MHC-Ib molecule, binds a very restricted repertoire of peptides, the peptide binding preferences of HLA-G, the class Ib molecule, are less stringent, although the basis by which HLA-G can bind various peptides is unclear. To investigate how HLA-G can accommodate different peptides, we compared the structure of HLA-G bound to three naturally abundant self-peptides (RIIPRHLQL, KGPPAALTL and KLPQAFYIL) and their thermal stabilities. The conformation of HLA-G(KGPPAALTL) was very similar to that of the HLA-G(RIIPRHLQL) structure. However, the structure of HLA-G(KLPQAFYIL) not only differed in the conformation of the bound peptide but also caused a small shift in the alpha2 helix of HLA-G. Furthermore, the relative stability of HLA-G was observed to be dependent on the nature of the bound peptide. These peptide-dependent effects on the substructure of the monomorphic HLA-G are likely to impact on its recognition by receptors of both innate and adaptive immune systems.
机译：高度多态的主要组织相容性复合体Ia类（MHC-Ia）分子为克隆型典型的字母T细胞受体提供了广泛的肽段。相反，MHC-Ib分子表现出有限的多态性并结合更受限制的肽库，与其在先天免疫中的主要作用保持一致。但是，某些MHC-Ib分子确实在适应性免疫中起作用。虽然人类白细胞抗原E（HLA-E）（MHC-Ib分子）结合了非常有限的肽库，但HLA-G（Ib类分子）的肽结合偏好并不那么严格，尽管HLA-G的基础G能否结合各种肽尚不清楚。为了研究HLA-G如何适应不同的肽，我们比较了与三种天然丰富的自身肽（RIIPRHLQL，KGPPAALTL和KLPQAFYIL）结合的HLA-G的结构及其热稳定性。 HLA-G（KGPPAALTL）的构象与HLA-G（RIIPRHLQL）结构的构象非常相似。但是，HLA-G（KLPQAFYIL）的结构不仅在结合的肽的构象上不同，而且引起了HLA-G的α2螺旋的微小变化。此外，观察到HLA-G的相对稳定性取决于结合的肽的性质。这些对单态HLA-G亚结构的肽依赖性作用可能会影响先天性和适应性免疫系统的受体对其的识别。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号