The papillomavirus E2 DNA binding domain.
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.
Instituto Leloir and IIBBA-CONICET, Av. Patricias Argentinas 435, (1405) Buenos Aires, Argentina. gpratgay@leloir.org.ar
Gonzalo
G
de Prat-Gay
Kevin
K
Gaston
Daniel O
DO
Cicero
D052685:Alphapapillomavirus / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D009154:Mutation; D027383:Papillomaviridae / Q000235:genetics / Q000378:metabolism*; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism
D004268:DNA-Binding Proteins; D014157:Transcription Factors; D014764:Viral Proteins