Utilize este identificador para referenciar este registo: http://hdl.handle.net/10400.7/478
Título: Structural basis for Z-DNA binding and stabilization by the zebrafish Z-DNA dependent protein kinase PKZ
Autor: de Rosa, M.
Zacarias, S.
Athanasiadis, A.
Palavras-chave: Amino Acid Sequence
DNA, Z-Form
Models, Molecular
Molecular Sequence Data
Protein Kinases
Protein Structure, Tertiary
Zebrafish Proteins
Data: 26-Jul-2013
Editora: Oxford University Press
Citação: Matteo de Rosa, Sonia Zacarias, and Alekos Athanasiadis Structural basis for Z-DNA binding and stabilization by the zebrafish Z-DNA dependent protein kinase PKZ Nucl. Acids Res. (2013) 41 (21): 9924-9933 first published online August 23, 2013 doi:10.1093/nar/gkt743
Resumo: The RNA-dependent protein kinase PKR plays a central role in the antiviral defense of vertebrates by shutting down protein translation upon detection of viral dsRNA in the cytoplasm. In some teleost fish, PKZ, a homolog of PKR, performs the same function, but surprisingly, instead of dsRNA binding domains, it harbors two Z-DNA/Z-RNA-binding domains belonging to the Zalpha domain family. Zalpha domains have also been found in other proteins, which have key roles in the regulation of interferon responses such as ADAR1 and DNA-dependent activator of IFN-regulatory factors (DAI) and in viral proteins involved in immune response evasion such as the poxviral E3L and the Cyprinid Herpesvirus 3 ORF112. The underlying mechanism of nucleic acids binding and stabilization by Zalpha domains is still unclear. Here, we present two crystal structures of the zebrafish PKZ Zalpha domain (DrZalpha(PKZ)) in alternatively organized complexes with a (CG)6 DNA oligonucleotide at 2 and 1.8 Å resolution. These structures reveal novel aspects of the Zalpha interaction with DNA, and they give insights on the arrangement of multiple Zalpha domains on DNA helices longer than the minimal binding site.
Peer review: yes
URI: http://hdl.handle.net/10400.7/478
DOI: 10.1093/nar/gkt743
Versão do Editor: http://nar.oxfordjournals.org/content/41/21/9924.long
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