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Structural basis for Z-DNA binding and stabilization by the zebrafish Z-DNA dependent protein kinase PKZ

2013-07-26Journal article Open access
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dc.contributor.authorde Rosa, M.
dc.contributor.authorZacarias, S.
dc.contributor.authorAthanasiadis, A.
dc.date.accessioned2015-11-09T16:26:50Z
dc.date.available2015-11-09T16:26:50Z
dc.date.issued2013-07-26
dc.description.abstractThe 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.pt_PT
dc.description.sponsorshipFCT fellowship: (SFRH/BPD/71629/2010), ESRF BAG program, Instituto Gulbenkian de Ciência.pt_PT
dc.identifier10.1093/nar/gkt743
dc.identifier.citationMatteo 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/gkt743pt_PT
dc.identifier.doi10.1093/nar/gkt743
dc.identifier.urihttp://hdl.handle.net/10400.7/478
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherOxford University Presspt_PT
dc.relationRecognition of Pathogen Nucleic Acids by Innate Immunity: Structure-Function Studies of the Cytoplasmic DNA Receptor DAI Pathway
dc.relationMolecular basis of the recognition of foreign nucleic acids in innate immunity
dc.relation.publisherversionhttp://nar.oxfordjournals.org/content/41/21/9924.longpt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectAmino Acid Sequencept_PT
dc.subjectDNA, Z-Formpt_PT
dc.subjectModels, Molecularpt_PT
dc.subjectMolecular Sequence Datapt_PT
dc.subjectProtein Kinasespt_PT
dc.subjectProtein Structure, Tertiarypt_PT
dc.subjectZebrafish Proteinspt_PT
dc.titleStructural basis for Z-DNA binding and stabilization by the zebrafish Z-DNA dependent protein kinase PKZpt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleRecognition of Pathogen Nucleic Acids by Innate Immunity: Structure-Function Studies of the Cytoplasmic DNA Receptor DAI Pathway
oaire.awardTitleMolecular basis of the recognition of foreign nucleic acids in innate immunity
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBIA-PRO%2F112962%2F2009/PT
oaire.awardURIinfo:eu-repo/grantAgreement/EC/FP7/231000/EU
oaire.citation.endPage9933pt_PT
oaire.citation.issue21pt_PT
oaire.citation.startPage9924pt_PT
oaire.citation.titleNucleic Acids Researchpt_PT
oaire.citation.volume41pt_PT
oaire.fundingStream3599-PPCDT
oaire.fundingStreamFP7
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100008530
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameEuropean Commission
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isProjectOfPublicationb6213c74-475a-49d7-8f04-445bf4da83fa
relation.isProjectOfPublication26aa4b1c-7402-432d-8bc2-bc68664311c3
relation.isProjectOfPublication.latestForDiscovery26aa4b1c-7402-432d-8bc2-bc68664311c3

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