不同核苷酸状态下KIF1A微管结合位点的结构变化
Structural Fluctuations of Microtubule Binding Site of KIF1A in Different Nucleotide States
摘要：
像驱动蛋白这样的分子马达如何在ATP水解过程中调节对rail蛋白的亲和力仍有待揭示。为了理解其调控机制，我们采用Go-like模型的分子动力学模拟研究了ATP水解过程中KIF1A在不同核苷酸状态下的结构波动.我们发现，作为微管（MT）结合位点的一部分的"α 4螺旋"根据核苷酸状态系统地改变其波动。特别是，α 4的大波动频率与KIF1A对微管的亲和力密切相关。我们还展示了热涨落的强度和与核苷酸的相互作用如何影响微管结合位点的动力学。这些结果表明，KIF1A通过根据核苷酸状态改变α 4螺旋的柔性来调节对MT的亲和力。
英文摘要：
How molecular motors like Kinesin regulates the affinity to the rail protein in the process of ATP hydrolysis remains to be uncovered. To understand the regulation mechanism, we investigate the structural fluctuation of KIF1A in different nucleotide states that are realized in the ATP hydrolysis process by molecular dynamics simulations of Go-like model. We found that "alpha4 helix", which is a part of the microtubule (MT) binding site, changes its fluctuation systematically according to the nucleotide states. In particular, the frequency of large fluctuations of alpha4 strongly correlates with the affinity of KIF1A for microtubule. We also show how the strength of the thermal fluctuation and the interaction with the nucleotide affect the dynamics of microtubule binding site. These results suggest that KIF1A regulates the affinity to MT by changing the flexibility of alpha4 helix according to the nucleotide states.
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