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4LB6

Crystal structure of PKZ Zalpha in complex with ds(CG)6 (tetragonal form)

Summary for 4LB6
Entry DOI10.2210/pdb4lb6/pdb
Related4LB5
DescriptorProtein kinase containing Z-DNA binding domains, 5'-D(*TP*CP*GP*CP*GP*CP*GP*CP*GP*CP*GP*CP*G)-3' (3 entities in total)
Functional Keywordswhth, zalpha, zbd, kinase, innate immunity, z-dna, z-rna, eif2a, transferase-dna complex, transferase/dna
Biological sourceDanio rerio (leopard danio,zebra danio,zebra fish)
More
Total number of polymer chains2
Total formula weight12420.14
Authors
De Rosa, M.,Zacarias, S.,Athanasiadis, A. (deposition date: 2013-06-20, release date: 2013-09-18, Last modification date: 2023-09-20)
Primary citationde Rosa, M.,Zacarias, S.,Athanasiadis, A.
Structural basis for Z-DNA binding and stabilization by the zebrafish Z-DNA dependent protein kinase PKZ.
Nucleic Acids Res., 41:9924-9933, 2013
Cited by
PubMed Abstract: 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.
PubMed: 23975196
DOI: 10.1093/nar/gkt743
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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건을2024-11-06부터공개중

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