2rvc

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'''Unreleased structure'''
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==Solution structure of Zalpha domain of goldfish ZBP-containing protein kinase==
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<StructureSection load='2rvc' size='340' side='right' caption='[[2rvc]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
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== Structural highlights ==
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<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>
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</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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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The entry 2rvc is ON HOLD until Paper Publication
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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>
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Authors: Lee, A., Park, C., Park, J., Kwon, M., Choi, Y., Kim, K., Choi, B., Lee, J.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Solution structure of Zalpha domain of goldfish ZBP-containing protein kinase
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<div class="pdbe-citations 2rvc" style="background-color:#fffaf0;"></div>
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[[Category: Unreleased Structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Choi, B]]
[[Category: Choi, Y]]
[[Category: Choi, Y]]
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[[Category: Kim, K]]
[[Category: Kwon, M]]
[[Category: Kwon, M]]
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[[Category: Choi, B]]
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[[Category: Lee, A]]
[[Category: Lee, J]]
[[Category: Lee, J]]
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[[Category: Lee, A]]
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[[Category: Park, C]]
[[Category: Park, J]]
[[Category: Park, J]]
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[[Category: Park, C]]
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[[Category: Dna binding protein]]
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[[Category: Kim, K]]
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[[Category: Helix turn helix]]
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[[Category: Z dna binding protein]]

Revision as of 15:35, 3 February 2016

Solution structure of Zalpha domain of goldfish ZBP-containing protein kinase

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