Ebola viral infections have resulted in several deadly epidemics in recent years in West and Central Africa. Because only one of the seven proteins encoded by the viral genome possesses enzymatic activity, disruption of protein–protein interactions is a promising route for antiviral drug development. We carried out a screening campaign to identify small, drug-like compounds that bind to the C-terminal region of the multifunctional Ebola nucleoprotein (eNP) with the objective of discovering ones that disrupt its binding to other Ebola proteins or to the single-stranded RNA genome. In the course of this effort we assigned the backbone ¹H, ¹⁵N, and ¹³C resonances of residues 600‒739, the region that contains the critical eVP30 binding region 600‒615 targeted by host factors, and used the assigned chemical shifts to predict secondary structural features and peptide dynamics. This work supports and extends the previous X-ray crystal structures and NMR studies of residues 641‒739. We found that the 600‒739 domain consists of separate regions that are largely disordered and ordered.

中文翻译：

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埃博拉核蛋白600-739构建体的骨干共振分配和二级结构。

近年来，埃博拉病毒感染在西非和中非造成了几起致命的流行病。由于病毒基因组编码的7种蛋白质中只有一种具有酶促活性，因此破坏蛋白质间相互作用是抗病毒药物开发的有希望的途径。我们进行了一项筛选活动，以鉴定与多功能埃博拉核蛋白（eNP）C端区域结合的小的药物样化合物，目的是发现破坏其与其他埃博拉病毒蛋白或单链结合的化合物RNA基因组。在此过程中，我们为主干分配了¹ H，¹⁵ N和¹³残基600‒739的C共振，该区域包含宿主因子靶向的关键eVP30结合区600‒615，并使用分配的化学位移预测二级结构特征和肽动力学。这项工作支持并扩展了先前的X射线晶体结构和641-739残基的NMR研究。我们发现600‒739域由很大程度上无序和有序的独立区域组成。