2rvc: Difference between revisions
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''' | ==Solution structure of Zalpha domain of goldfish ZBP-containing protein kinase== | ||
<StructureSection load='2rvc' size='340' side='right' caption='[[2rvc]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2rvc]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RVC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RVC FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rvc OCA], [http://pdbe.org/2rvc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rvc RCSB], [http://www.ebi.ac.uk/pdbsum/2rvc PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2rvc" style="background-color:#fffaf0;"></div> | |||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Choi, B]] | |||
[[Category: Choi, Y]] | [[Category: Choi, Y]] | ||
[[Category: Kim, K]] | |||
[[Category: Kwon, M]] | [[Category: Kwon, M]] | ||
[[Category: | [[Category: Lee, A]] | ||
[[Category: Lee, J]] | [[Category: Lee, J]] | ||
[[Category: | [[Category: Park, C]] | ||
[[Category: Park, J]] | [[Category: Park, J]] | ||
[[Category: | [[Category: Dna binding protein]] | ||
[[Category: | [[Category: Helix turn helix]] | ||
[[Category: Z dna binding protein]] | |||