• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >Structure of internalin InlK from the human pathogen listeria monocytogenes
【24h】

Structure of internalin InlK from the human pathogen listeria monocytogenes

机译：人类病原体单核细胞增生李斯特氏菌Internalin InlK的结构

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

Listeria monocytogenes is a human pathogen that employs a wide variety of virulence factors in order to adhere to, invade, and replicate within target cells. Internalins play key roles in processes ranging from adhesion to receptor recognition and are thus essential for infection. Recently, InlK, a surface-associated internalin, was shown to be involved in Listeria's ability to escape from autophagy by recruitment of the major vault protein (MVP) to the bacterial surface. Here, we report the structure of InlK, which harbors four domains arranged in the shape of a "bent arm". The structure supports a role for the "elbow" of InlK in partner recognition, as well as of two Ig-like pedestals intercalated by hinge regions in the projection of InlK away from the surface of the bacterium. The unusual fold and flexibility of InlK could be essential for MVP binding and concealment from recognition by molecules involved in the autophagic process.
机译：单核细胞增生李斯特菌是一种人类病原体，它利用多种毒力因子粘附，侵袭并在靶细胞内复制。在从粘附到受体识别的过程中，Internalins起着关键作用，因此对于感染至关重要。最近，InlK（一种与表面相关的internalin）被证明参与了李斯特菌（Listeria）通过将主要穹protein蛋白（MVP）募集到细菌表面而自噬的能力。在这里，我们报告InlK的结构，该结构包含四个以“弯曲臂”形状排列的域。该结构支持InlK的“肘”在伙伴识别中的作用，以及两个IngK远离细菌表面的投影中的铰链区插入的Ig状基座。 InlK的异常折叠和柔韧性可能对于MVP结合和隐藏自噬过程涉及的分子的识别至关重要。

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