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首页> 外文期刊>Biochemistry >Relaxation-based structure refinement and backbone molecular dynamics of the Dynein motor domain-associated light chain.
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Relaxation-based structure refinement and backbone molecular dynamics of the Dynein motor domain-associated light chain.

机译：与Dynein马达域相关的轻链的基于松弛的结构细化和主链分子动力学。

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摘要

The light chain 1 (LC1) polypeptide is a member of the leucine-rich repeat protein family and binds at or near the ATP hydrolytic site within the motor domain of the gamma heavy chain from Chlamydomonas outer arm dynein. It consists of an N-terminal helix, a central barrel formed from six leucine-rich repeats that fold as betabetaalpha units, and a C-terminal helical domain that protrudes from the main axis defined by the leucine-rich repeats. Interaction with the gamma heavy chain is likely mediated through a hydrophobic patch on the larger beta sheet face, and the C-terminal region is predicted to insert into the dynein ATP hydrolytic site. Here we have used (1)H-(15)N heteronuclear relaxation measurements obtained at 500 and 600 MHz to refine and validate the LC1 solution structure. In this refined structure, the C-terminal helix is significantly reoriented by more than 20 degrees as compared to the control and provides a more precise understanding of the potential regulatory role of this domain. Wealso employed the refined structure to perform a dynamic analysis of LC1 using the 600 MHz data set. These results, which were cross validated using the 500 MHz data set, strongly support identification of the predicted LC1 binding surfaces and provide additional insight into the interaction mechanisms of leucine-rich repeat proteins.
机译：轻链1（LC1）多肽是富含亮氨酸的重复蛋白家族的成员，在衣藻衣藻外臂动力蛋白的γ重链运动域内的ATP水解位点处或附近结合。它由一个N末端螺旋，一个由六个富含亮氨酸的重复序列折叠成βbetaalpha单元的中央桶和一个从富含亮氨酸的重复序列所定义的主轴突出的C末端螺旋结构域组成。与γ重链的相互作用可能是通过较大的β片层表面上的疏水性补丁介导的，预计C末端区域将插入到动力蛋白ATP水解位点。在这里，我们使用在500和600 MHz处获得的（1）H-（15）N异核弛豫测量值来完善和验证LC1解决方案的结构。在这种精致的结构中，与对照相比，C末端螺旋线显着重定向了20度以上，并提供了对该域潜在调节作用的更精确的理解。我们还使用改进的结构使用600 MHz数据集对LC1进行了动态分析。这些结果，使用500 MHz数据集进行了交叉验证，有力地支持了对预测的LC1结合表面的鉴定，并提供了对富含亮氨酸的重复蛋白相互作用机制的进一步了解。

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