2rvc

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rvc OCA], [https://pdbe.org/2rvc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rvc RCSB], [https://www.ebi.ac.uk/pdbsum/2rvc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rvc ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Z-DNA binding proteins (ZBPs) play important roles in RNA editing, innate immune response and viral infection. Structural and biophysical studies show that ZBPs initially form an intermediate complex with B-DNA for B-Z conversion. However, a comprehensive understanding of the mechanism of Z-DNA binding and B-Z transition is still lacking, due to the absence of structural information on the intermediate complex. Here, we report the solution structure of the Zalpha domain of the ZBP-containing protein kinase from Carassius auratus (caZalphaPKZ). We quantitatively determined the binding affinity of caZalphaPKZ for both B-DNA and Z-DNA and characterized its B-Z transition activity, which is modulated by varying the salt concentration. Our results suggest that the intermediate complex formed by caZalphaPKZ and B-DNA can be used as molecular ruler, to measure the degree to which DNA transitions to the Z isoform.

Solution structure of the Z-DNA binding domain of PKR-like protein kinase from Carassius auratus and quantitative analyses of the intermediate complex during B-Z transition.,Lee AR, Park CJ, Cheong HK, Ryu KS, Park JW, Kwon MY, Lee J, Kim KK, Choi BS, Lee JH Nucleic Acids Res. 2016 Jan 20. pii: gkw025. PMID:26792893<ref>PMID:26792893</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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