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Structural and Dynamic Characterization of the Molecular Hub Early Region 1A (E1A) from Human Adenovirus
Author(s) -
Hošek Tomáš,
Calçada Eduardo O.,
Nogueira Marcela Oliveira,
Salvi Michele,
Pagani Talita Duarte,
Felli Isabella C.,
Pierattelli Roberta
Publication year - 2016
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201602510
Subject(s) - computational biology , characterization (materials science) , gene isoform , biology , gene , genetics , nanotechnology , materials science
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.