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首页> 外文期刊>Journal of Molecular Biology >Association of nuclear pore FG-repeat domains to NTF2 import and export complexes
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Association of nuclear pore FG-repeat domains to NTF2 import and export complexes

机译：核孔FG重复域与NTF2进出口复合物的关联

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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.
机译：进出核的转运受核孔复合物调节。该调节的关键是具有FG序列重复的核孔蛋白，这些蛋白对细胞活力至关重要，并且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Ran进口商NTF2表面的结合。该模拟覆盖了254 ns以上，与先前的X射线，突变，NMR和计算数据在确定四个结合点时相吻合。它们还用于提供每个位置上结合的全原子视图，而FG重复结合仅在单个位置上直接观察到。此外，模拟识别了另外四个其他的两个新的结合点。所有六个结合点在NTF2的整个表面上广泛形成条纹。对于通过核孔复合物中的FG重复识别转运受体以及成功地使NTF2穿过孔，可能需要表面上形成的结合点规则性和邻近性。 （c）2006 Elsevier Ltd.版权所有。

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