期刊
VIROLOGY
卷 525, 期 -, 页码 117-131出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2018.08.012
关键词
Adenovirus; E1A; Intrinsic disorder; Linear motifs; Motif repertoire; Sequence conservation; Co-evolution; Random polymer
类别
资金
- Agencia Nacional de Promotion Cientifica y Tecnologica [PICT 2012-2550, PICT 2015-1213, PICT 2013-1895]
- Consejo Nacional de Investigaciones Cientificas y Tecnicas [11220130100558CO]
E1A is the main transforming protein in mastadenoviruses. This work uses bioinformatics to extrapolate experimental knowledge from Human adenovirus serotype 5 and 12 E1A proteins to all known serotypes. A conserved domain architecture with a high degree of intrinsic disorder acts as a scaffold for multiple linear motifs with variable occurrence mediating the interaction with over fifty host proteins. While linear motifs contribute strongly to sequence conservation within intrinsically disordered E1A regions, motif repertoires can deviate significantly from those found in prototypical serotypes. Close to one hundred predicted residue-residue contacts suggest the presence of stable structure in the CR3 domain and of specific conformational ensembles involving both short- and long-range intramolecular interactions. Our computational results suggest that E1A sequence conservation and co-evolution reflect the evolutionary pressure to maintain a mainly disordered, yet non-random conformation harboring a high number of binding motifs that mediate viral hijacking of the cell machinery.
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