| Literature DB >> 27490777 |
Tomáš Hošek1, Eduardo O Calçada1, Marcela Oliveira Nogueira1, Michele Salvi1, Talita Duarte Pagani1, Isabella C Felli2, Roberta Pierattelli3.
Abstract
The small-DNA human adenovirus encodes one of the most versatile molecular hubs, the E1A protein. This protein is essential for productive viral infection in human cells and a vast amount of biologically relevant data are available on its interactions with host proteins. Up to now, however, no high-resolution structural and dynamic information on E1A is available despite its important biological role. Among the different spliced variants of E1A, two are expressed at high level in the early stage of infection. These are 243 and 289 residues isoforms. Herein, we present their NMR characterization, showing that they are both highly disordered, but also demonstrate a certain heterogeneous behavior in terms of structural and dynamic properties. Furthermore, we present the characterization of the isolated domain of the longer variant, known as CR3. This study opens the way to understanding at the molecular level how E1A functions.Entities:
Keywords: NMR spectroscopy; human adenovirus; intrinsically disordered proteins (IDP); molecular hub; viral proteins
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Year: 2016 PMID: 27490777 DOI: 10.1002/chem.201602510
Source DB: PubMed Journal: Chemistry ISSN: 0947-6539 Impact factor: 5.236