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首页> 外文期刊>Biochemistry >Interesting Structural and Dynamical Behaviors Exhibited by the AF-6 PDZ Domain upon Bcr Peptide Binding
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Interesting Structural and Dynamical Behaviors Exhibited by the AF-6 PDZ Domain upon Bcr Peptide Binding

机译：AF-6 PDZ域在Bcr肽结合后表现出的有趣的结构和动力学行为

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摘要

PDZ (postsynaptic density-95, disks large, zonula occludens-1) domains are small, protein-protein interaction modules that have multiple binding surfaces for the docking of diverse molecules. These domains can propagate signals from ligand-binding site to distal regions of the structure through allosteric communication. Recent works have revealed that picosecond to nanosecond time scale dynamics play a potential role in propagating long-range signals within a protein. Comparison of AF-6 PDZ domain structures in free and complex forms shows a conformation rearrangement of distal surface 2, which is far from the peptide binding groove. The relaxation dispersion experiments detected that the free AF-6 PDZ domain was sampling multiple conformations; millisecond dynamics mapped a network for allostery signal transmission throughout the AF-6 PDZ domain in the weak saturation state, and intramolecular motions were observed in distal surface 1 when the protein was saturated. These results provide evidence that the allosteric process in the AF-6 PDZ domain is not two-state; instead, the millisecond dynamic network provides a mechanism for the transmission of allosteric signals throughout a protein. Interestingly, the two distal surfaces of the AF-6 PDZ domain respond differently to peptide binding; distal surface 1 changes in millisecond dynamics, whereas distal surface 2 undergoes structural rearrangement. The significance of the different response patterns in the signaling pathway and its relevance to the function of the AF-6 PDZ domain should be studied further.
机译：PDZ（突触后密度为95，盘大，小带闭合）-1域是小的蛋白质-蛋白质相互作用模块，具有多个结合表面，可用于对接不同的分子。这些结构域可以通过变构通讯将信号从配体结合位点传播到结构的远端区域。最近的研究表明，皮秒至纳秒级的时间尺度动力学在蛋白质中传播远距离信号方面具有潜在作用。游离和复杂形式的AF-6 PDZ域结构的比较显示远侧表面2的构象重排，该表面重排远离肽结合槽。弛豫分散实验检测到，游离的AF-6 PDZ域正在采样多个构象。毫秒级动力学绘制了一个网络，用于在弱饱和状态下整个AF-6 PDZ域中的变构信号传输网络，当蛋白质饱和时，在远端表面1观察到了分子内运动。这些结果提供了证据，表明AF-6 PDZ域中的变构过程不是两个状态。取而代之的是，毫秒级动态网络为整个蛋白质中的变构信号传输提供了一种机制。有趣的是，AF-6 PDZ结构域的两个远端表面对肽结合的反应不同。远端表面1以毫秒为单位变化，而远端表面2进行结构重排。信号通路中不同应答模式的重要性及其与AF-6 PDZ域功能的相关性应进一步研究。

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