Hošek Tomáš, Calçada Eduardo O, Nogueira Marcela Oliveira, Salvi Michele, Pagani Talita Duarte, Felli Isabella C, Pierattelli Roberta
CERM and Department of Chemistry "Ugo Schiff", University of Florence, via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy.
Chemistry. 2016 Sep 5;22(37):13010-3. doi: 10.1002/chem.201602510. Epub 2016 Aug 4.
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.
小型DNA人类腺病毒编码了一种最具多功能性的分子枢纽——E1A蛋白。这种蛋白对于人类细胞中的有效病毒感染至关重要，并且关于其与宿主蛋白相互作用的大量生物学相关数据是可得的。然而，尽管E1A具有重要的生物学作用，但到目前为止，尚无关于它的高分辨率结构和动态信息。在E1A的不同剪接变体中，有两种在感染早期高水平表达。它们是243和289个残基的异构体。在此，我们展示了它们的核磁共振表征，表明它们都高度无序，但在结构和动态特性方面也表现出一定的异质性。此外，我们展示了较长变体的分离结构域（称为CR3）的表征。这项研究为在分子水平上理解E1A的功能开辟了道路。
