The small DNA tumor viruses encode some of the most versatile hub proteins like the E1A protein from human Adenovirus (HAdV). The E1A protein is essential for productive viral infection in human cells and a vast amount of data are available on its interactions with host proteins. Up to now no high-resolution information on the full-length E1A protein is available despite its important biological role. Here we present the NMR characterization of the entire 243 residue long 12S isoform of the E1A protein from HAdV (E1A-12S). The protein results very heterogeneous in terms of structural and dynamic properties with highly flexible modules. This study opens the way to characterize the many interactions in which this protein is involved.
Poster Sessions - The highly flexible and heterogeneous nature of E1A from human Adenovirus (HAdV) characterized at atomic resolution through NMR / Isabella Caterina Felli. - In: THE FEBS JOURNAL. - ISSN 1742-464X. - STAMPA. - 281:(2014), pp. 65-784. [10.1111/febs.12919]
Poster Sessions - The highly flexible and heterogeneous nature of E1A from human Adenovirus (HAdV) characterized at atomic resolution through NMR
Isabella Caterina FelliWriting – Original Draft Preparation
2014
Abstract
The small DNA tumor viruses encode some of the most versatile hub proteins like the E1A protein from human Adenovirus (HAdV). The E1A protein is essential for productive viral infection in human cells and a vast amount of data are available on its interactions with host proteins. Up to now no high-resolution information on the full-length E1A protein is available despite its important biological role. Here we present the NMR characterization of the entire 243 residue long 12S isoform of the E1A protein from HAdV (E1A-12S). The protein results very heterogeneous in terms of structural and dynamic properties with highly flexible modules. This study opens the way to characterize the many interactions in which this protein is involved.I documenti in FLORE sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.



