de Prat-Gay Gonzalo, Gaston Kevin, Cicero Daniel O
Instituto Leloir and IIBBA-CONICET, Av. Patricias Argentinas 435, (1405) Buenos Aires, Argentina.
Front Biosci. 2008 May 1;13:6006-21. doi: 10.2741/3132.
The DNA binding domain of the E2 master regulator from papillomaviruses is the primary effector for most the essential activities controlled by this protein. In this review we focus on the properties of the DNA binding domain of human papillomavirus strain 16 in solution, integrating structure, dynamics, folding, stability, conformational equilibria, and DNA binding mechanism. We discuss the relevance of these processes for the different biological activities, broadening the horizon for antiviral development. In addition, the particular fold of the DNA binding domain only shared with the Epstein-Barr nuclear antigen EBNA1, suggests a link between this unique architecture and the function of viral origin binding proteins of this kind. Finally, the E2 DNA binding domain proved to be an excellent model for addressing fundamental problems of DNA recognition mechanisms and folding of intertwined dimers.
乳头瘤病毒E2主调节因子的DNA结合结构域是该蛋白控制的大多数基本活动的主要效应器。在本综述中，我们聚焦于溶液中人类乳头瘤病毒16型DNA结合结构域的特性，综合探讨其结构、动力学、折叠、稳定性、构象平衡及DNA结合机制。我们讨论了这些过程与不同生物学活性的相关性，拓宽了抗病毒研发的视野。此外，DNA结合结构域的特殊折叠仅与爱泼斯坦-巴尔核抗原EBNA1相同，这表明这种独特结构与这类病毒起源结合蛋白的功能之间存在联系。最后，E2 DNA结合结构域被证明是解决DNA识别机制和交织二聚体折叠等基本问题的优秀模型。
