Utilize este identificador para referenciar este registo: http://hdl.handle.net/10400.7/484
Título: Crystal structure of a poxvirus-like zalpha domain from cyprinid herpesvirus 3
Autor: Tomé, Ana Rita
Kuś, Krzysztof
Correia, Silvia
Paulo, Lara Martins
Zacarias, Sónia
de Rosa, Matteo
Figueiredo, Delio
Parkhouse, R Michael E
Athanasiadis, Alekos
Palavras-chave: Chromatography, Gel
Cloning, Molecular
CpG Islands
Crystallography
DNA Viruses
Dimerization
Open Reading Frames
Protein Folding
Viral Proteins
Models, Molecular
Protein Conformation
Data: Abr-2013
Editora: American Society for Microbiology
Citação: Crystal Structure of a Poxvirus-Like Zalpha Domain from Cyprinid Herpesvirus 3 Ana Rita Tomé, Krzysztof Kuś, Silvia Correia, Lara Martins Paulo, Sónia Zacarias, Matteo de Rosa, Delio Figueiredo, R. Michael E. Parkhouse, and Alekos Athanasiadis J. Virol. April 2013 87:7 3998-4004; Accepted manuscript posted online 30 January 2013, doi:10.1128/JVI.03116-12
Resumo: Zalpha domains are a subfamily of the winged helix-turn-helix domains sharing the unique ability to recognize CpG repeats in the left-handed Z-DNA conformation. In vertebrates, domains of this family are found exclusively in proteins that detect foreign nucleic acids and activate components of the antiviral interferon response. Moreover, poxviruses encode the Zalpha domain-containing protein E3L, a well-studied and potent inhibitor of interferon response. Here we describe a herpesvirus Zalpha-domain-containing protein (ORF112) from cyprinid herpesvirus 3. We demonstrate that ORF112 also binds CpG repeats in the left-handed conformation, and moreover, its structure at 1.75 Å reveals the Zalpha fold found in ADAR1, DAI, PKZ, and E3L. Unlike other Zalpha domains, however, ORF112 forms a dimer through a unique domain-swapping mechanism. Thus, ORF112 may be considered a new member of the Z-domain family having DNA binding properties similar to those of the poxvirus E3L inhibitor of interferon response.
Peer review: yes
URI: http://hdl.handle.net/10400.7/484
DOI: 10.1128/JVI.03116-12
Versão do Editor: http://jvi.asm.org/content/87/7/3998.long
Aparece nas colecções:PNAI - Artigos
II- Artigos

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