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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Principles underlying energetic coupling along an allosteric communication trajectory of a voltage-activated K~+ channel
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Principles underlying energetic coupling along an allosteric communication trajectory of a voltage-activated K~+ channel

机译：沿电压激活的K〜+通道的变构通讯轨迹进行能量耦合的基本原理

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摘要

The information flow between distal elements of a protein may rely on allosteric communication trajectories lying along the protein's tertiary or quaternary structure. To unravel the underlying features of energy parsing along allosteric pathways in voltage-gated K~+ channels, high-order thermodynamic coupling analysis was performed. We report that such allosteric trajectories are functionally conserved and delineated by well defined boundaries. Moreover, allosteric trajectories assume a hierarchical organization whereby increasingly stronger layers of cooperative residue interactions act to ensure efficient and cooperative long-range coupling between distal channel regions. Such long-range communication is brought about by a coupling of local and global conformational changes, suggesting that the allosteric trajectory also corresponds to a pathway of physical deformation. Supported by theoretical analyses and analogy to studies analyzing the contribution of long-range residue coupling to protein stability, we propose that such experimentally derived trajectory features are a general property of allosterically regulated proteins.
机译：蛋白质远端元件之间的信息流可能依赖于沿着蛋白质三级或四级结构的变构通讯轨迹。为了揭示沿电压门控K +通道中变构途径的能量解析的潜在特征，进行了高阶热力学耦合分析。我们报告这样的变构轨迹在功能上是守恒的，并由明确定义的边界来描绘。此外，变构轨迹采用分级组织，由此协作残基相互作用的越来越强的层起作用以确保远端通道区域之间的有效且协作的远程耦合。这种远程通讯是通过局部和整体构象变化的耦合而实现的，这表明变构轨迹也对应于物理变形的路径。在理论分析和类比分析的支持下，我们对长期残基偶联对蛋白质稳定性的影响进行了分析，我们提出这种实验得出的轨迹特征是变构调节蛋白质的一般特性。

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