The domain 2 of the HCV NS5A protein is intrinsically unstructured.
The domain 2 of the HCV NS5A protein is intrinsically unstructured.
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HCV NS5A 蛋白的结构域 2 本质上是非结构化的。
DOI：
10.2174/0929210204504848665
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发表时间：
2010
影响因子：
1.6
通讯作者：
G. Lippens
中科院分区：
文献类型：
--
作者：
X. Hanoulle;Aurélie Badillo;Dries Verdegem;F. Penin;G. Lippens
我们在此介绍目前对丙型肝炎病毒 NS5A-D2 结构域的了解。尽管通过尺寸排阻色谱、圆二色性和同核核磁共振光谱等宏观技术评估，该蛋白质结构域总体上是非结构化的，但高分辨率三重共振光谱可以识别残留结构的小区域。此外，该区域对应于病毒不同基因型中最保守的序列，强调了其功能重要性。我们证明它形成了宿主细胞亲环蛋白脯氨酰顺/反异构酶的锚定点，为在抗病毒策略中使用亲环蛋白抑制剂提供了分子基础。
We present here our current understanding of the NS5A-D2 domain of the hepatitis C virus. Whereas this protein domain is globally unstructured as assessed by macroscopic techniques such as size exclusion chromatography, circular dichroism and homonuclear NMR spectroscopy, high resolution triple resonance spectroscopy allows the identification of a small region of residual structure. This region corresponds moreover to the most conserved sequence over the different genotypes of the virus, underscoring its functional importance. We show that it forms an anchoring point for the host cell cyclophilin prolyl cis/trans isomerase, providing a molecular basis for the use of cyclophilin inhibitors in an antiviral strategy.