The hepatitis C virus NS3 protein: a model RNA helicase and potential drug target.
The hepatitis C virus NS3 protein: a model RNA helicase and potential drug target.
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DOI：
10.21775/cimb.009.001
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发表时间：
2007
影响因子：
3.1
通讯作者：
D. Frick
中科院分区：
文献类型：
--
作者：
D. Frick
丙型肝炎病毒（HCV）非结构蛋白3 （NS3）的C端部分形成一个三结构域多肽，具有沿RNA或单链DNA （ssDNA）沿3‘至5’方向移动的能力。在atp水解的推动下，这种运动允许蛋白质取代与核酸结合的DNA或RNA和蛋白质的互补链。HCV解旋酶与其他运动蛋白有两个共同的结构域，其中一个似乎在ATP结合时旋转。已经提出了几种模型来解释这种构象变化如何导致蛋白质运动和RNA解绕，但目前没有模型可以解释所有现有的实验数据。最近报道的抑制HCV解旋酶的化合物，包括许多小分子、RNA适体和抗体，将有助于阐明解旋酶在正意义单链RNA病毒复制中的作用，并可能作为设计新型抗病毒药物的模板。
The C-terminal portion of hepatitis C virus (HCV) nonstructural protein 3 (NS3) forms a three domain polypeptide that possesses the ability to travel along RNA or single-stranded DNA (ssDNA) in a 3' to 5' direction. Fueled byATP hydrolysis, this movement allows the protein to displace complementary strands of DNA or RNA and proteins bound to the nucleic acid. HCV helicase shares two domains common to other motor proteins, one of which appears to rotate upon ATP binding. Several models have been proposed to explain how this conformational change leads to protein movement and RNA unwinding, but no model presently explains all existing experimental data. Compounds recently reported to inhibit HCV helicase, which include numerous small molecules, RNA aptamers and antibodies, will be useful for elucidating the role of a helicase in positive-sense single-stranded RNA virus replication and might serve as templates for the design of novel antiviral drugs.