• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >Crystal structure of a non-canonical low-affinity peptide complexed with MHC class I: a new approach for vaccine design.
【24h】

Crystal structure of a non-canonical low-affinity peptide complexed with MHC class I: a new approach for vaccine design.

机译：与MHC I类复合的非规范性低亲和力肽的晶体结构：疫苗设计的新方法。

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

Peptides bind with high affinity to MHC class I molecules by anchoring certain side-chains (anchors) into specificity pockets in the MHC peptide-binding groove. Peptides that do not contain these canonical anchor residues normally have low affinity, resulting in impaired pMHC stability and loss of immunogenicity. Here, we report the crystal structure at 1.6 A resolution of an immunogenic, low-affinity peptide from the tumor-associated antigen MUC1, bound to H-2Kb. Stable binding is still achieved despite small, non-canonical residues in the C and F anchor pockets. This structure reveals how low-affinity peptides can be utilized in the design of novel peptide-based tumor vaccines. The molecular interactions elucidated in this non-canonical low-affinity peptide MHC complex should help uncover additional immunogenic peptides from primary protein sequences and aid in the design of alternative approaches for T-cell vaccines.
机译：肽通过将某些侧链（锚）锚定在MHC肽结合槽的特异性口袋中而与MHC I类分子高亲和力结合。不包含这些规范锚残基的肽通常具有低亲和力，从而导致pMHC稳定性受损和免疫原性丧失。在这里，我们报道了来自肿瘤相关抗原MUC1的，与H-2Kb结合的免疫原性，低亲和力肽的1.6 A分辨率的晶体结构。尽管在C和F锚袋中有小的非规范残基，仍然可以实现稳定的结合。这种结构揭示了如何在基于肽的新型肿瘤疫苗设计中利用低亲和力肽。这种非规范的低亲和力肽MHC复合体中阐明的分子相互作用应有助于从一级蛋白质序列中发现其他免疫原性肽，并有助于设计T细胞疫苗的替代方法。

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