...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochemistry >Structure and topology of diphtheria toxin R domain in lipid membranes.
【24h】

Structure and topology of diphtheria toxin R domain in lipid membranes.

机译：脂质膜中白喉毒素R结构域的结构和拓扑。

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 interaction of the receptor-binding domain (R domain) of diphtheria toxin with a pure lipid membrane has been characterized by several approaches. Using a photoactivatable lipid, the R domain has been shown to deeply insert in the lipid membrane. Three regions of the R domain (residues 380-421, 422-441, and 442 to about 483) are protected by their interaction with the membrane from externally added proteases. At least one of these regions is deeply interacting with the lipid membrane, as evidenced by the location of Cys 461 and 471 determined by fluorescence experiments. Binding of the R domain to the lipid membrane is characterized by the appearance of an alpha-helical component whose orientation is compatible with a transmembrane orientation.
机译：白喉毒素的受体结合结构域（R结构域）与纯脂质膜的相互作用已通过几种方法进行了表征。使用可光活化的脂质，R结构域已显示出可深度插入脂质膜中。 R结构域的三个区域（残基380-421、422-441和442至约483）通过与膜的相互作用而免受外部添加的蛋白酶的影响。这些区域中的至少一个与脂质膜深度相互作用，如通过荧光实验确定的Cys 461和471的位置所证明的。 R结构域与脂质膜的结合的特征在于其α-螺旋组分的取向与跨膜取向相容。

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