Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.
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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.