Association of nuclear pore FG-repeat domains to NTF2 import and export complexes
Association of nuclear pore FG-repeat domains to NTF2 import and export complexes
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DOI：
10.1016/j.jmb.2006.11.048
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发表时间：
2007-02-09
影响因子：
5.6
通讯作者：
Schulten, Klaus
中科院分区：
文献类型：
--
作者：
Isgro, Timothy A.;Schulten, Klaus
核孔复合物调节细胞核的进出运输。对这种调节至关重要的是具有FG序列重复的核孔蛋白，其已被证明对细胞活力至关重要，并与核转运受体相互作用。在这里，我们使用分子动力学模拟来研究FG-重复肽与NTF 2表面的结合，NTF 2是Ran进口商。模拟，覆盖超过254纳秒，同意与以前的X射线，突变，NMR和计算数据，确定四个结合点。它们还用于提供每个点处结合的全原子视图，而FG-重复序列结合仅在单个点处直接观察到。此外，模拟确定两个新的结合点，除了其他四个。所有六个结合点在NTF 2的表面上广泛地形成条带。所得到的规律性和接近的表面上的结合点可能是必要的识别的运输受体的核孔复合物中的FG-重复序列，并成功的运输NTF 2通过孔。(c)2006爱思唯尔有限公司版权所有。
Transport into and out of the nucleus is regulated by the nuclear pore complex. Vital to this regulation are nuclear pore proteins with FG sequence repeats, which have been shown to be crucial for cell viability and which interact with nuclear transport receptors. Here we use molecular dynamics simulations to investigate the binding of FG-repeat peptides to the surface of NTF2, the Ran importer. The simulations, covering over 254 ns, agree with previous X-ray, mutational, NMR, and computational data in identifying four binding spots. They also serve to provide an all-atom view of binding at each spot, whereas FG-repeat binding has been only directly observed at a single spot. Furthermore, the simulations identify two novel binding spots in addition to the four others. All six binding spots broadly form a stripe across the surface of NTF2. The resulting regularity and proximity of binding spots on the surface may be necessary for identification of the transport receptor by the FG-repeats in the nuclear pore complex and for the successful transit of NTF2 through the pore. (c) 2006 Elsevier Ltd. AN rights reserved.