...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochemistry >Structures of the excited states of phospholamban and shifts in their populations upon phosphorylation
【24h】

Structures of the excited states of phospholamban and shifts in their populations upon phosphorylation

机译：磷酸lamban的激发态结构及其在磷酸化后的种群迁移

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

Phospholamban is an integral membrane protein that controls the calcium balance in cardiac muscle cells. As the function and regulation of this protein require the active involvement of low populated states in equilibrium with the native state, it is of great interest to acquire structural information about them. In this work, we calculate the conformations and populations of the ground state and the three main excited states of phospholamban by incorporating nuclear magnetic resonance residual dipolar couplings as replica-averaged structural restraints in molecular dynamics simulations. We then provide a description of the manner in which phosphorylation at Ser16 modulates the activity of the protein by increasing the sizes of the populations of its excited states. These results demonstrate that the approach that we describe provides a detailed characterization of the different states of phospholamban that determine the function and regulation of this membrane protein. We anticipate that the knowledge of conformational ensembles enable the design of new dominant negative mutants of phospholamban by modulating the relative populations of its conformational substates.
机译：Phospholamban是控制心肌细胞中钙平衡的不可或缺的膜蛋白。由于这种蛋白质的功能和调节要求低种群状态与天然状态保持平衡，因此积极寻求有关其的结构信息。在这项工作中，我们通过将核磁共振残余偶极偶合作为分子动力学模拟中复制平均结构约束，计算了磷lamban的基态和三个主要激发态的构象和总体。然后，我们提供Ser16磷酸化通过增加其激发态群体的大小来调节蛋白质活性的方式的描述。这些结果表明，我们描述的方法提供了决定该膜蛋白功能和调控的磷酸lamban的不同状态的详细表征。我们预期构象知识的集成能够通过调节其构象亚状态的相对种群来设计磷酸lamban的新的显性负突变体。

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