DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, Ae-Ree | ko |
dc.contributor.author | Park, Chin-Ju | ko |
dc.contributor.author | Cheong, Hae-Kap | ko |
dc.contributor.author | Ryu, Kyoung-Seok | ko |
dc.contributor.author | Park, Jin-Wan | ko |
dc.contributor.author | Kwon, Mun-Young | ko |
dc.contributor.author | Lee, Janghyun | ko |
dc.contributor.author | Kim, Kyeong Kyu | ko |
dc.contributor.author | Choi, Byong-Seok | ko |
dc.contributor.author | Lee, Joon-Hwa | ko |
dc.date.accessioned | 2016-07-06T04:24:23Z | - |
dc.date.available | 2016-07-06T04:24:23Z | - |
dc.date.created | 2016-06-08 | - |
dc.date.created | 2016-06-08 | - |
dc.date.issued | 2016-04 | - |
dc.identifier.citation | NUCLEIC ACIDS RESEARCH, v.44, no.6, pp.2936 - 2948 | - |
dc.identifier.issn | 0305-1048 | - |
dc.identifier.uri | http://hdl.handle.net/10203/209538 | - |
dc.description.abstract | 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 Z alpha domain of the ZBP-containing protein kinase from Carassius auratus (caZ alpha(PKZ)). We quantitatively determined the binding affinity of caZ alpha(PKZ) 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 caZ alpha(PKZ) and B-DNA can be used as molecular ruler, to measure the degree to which DNA transitions to the Z isoform | - |
dc.language | English | - |
dc.publisher | OXFORD UNIV PRESS | - |
dc.subject | Z-ALPHA DOMAIN | - |
dc.subject | HANDED Z-DNA | - |
dc.subject | NUCLEAR-MAGNETIC-RESONANCE | - |
dc.subject | HUMAN EDITING ENZYME | - |
dc.subject | MOLECULAR-CLONING | - |
dc.subject | CRYSTAL-STRUCTURE | - |
dc.subject | PROTON-EXCHANGE | - |
dc.subject | HUMAN ADAR1 | - |
dc.subject | NMR SYSTEM | - |
dc.subject | CELLS | - |
dc.title | 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 | - |
dc.type | Article | - |
dc.identifier.wosid | 000374570500045 | - |
dc.identifier.scopusid | 2-s2.0-84963946762 | - |
dc.type.rims | ART | - |
dc.citation.volume | 44 | - |
dc.citation.issue | 6 | - |
dc.citation.beginningpage | 2936 | - |
dc.citation.endingpage | 2948 | - |
dc.citation.publicationname | NUCLEIC ACIDS RESEARCH | - |
dc.identifier.doi | 10.1093/nar/gkw025 | - |
dc.contributor.localauthor | Choi, Byong-Seok | - |
dc.contributor.nonIdAuthor | Lee, Ae-Ree | - |
dc.contributor.nonIdAuthor | Park, Chin-Ju | - |
dc.contributor.nonIdAuthor | Cheong, Hae-Kap | - |
dc.contributor.nonIdAuthor | Ryu, Kyoung-Seok | - |
dc.contributor.nonIdAuthor | Park, Jin-Wan | - |
dc.contributor.nonIdAuthor | Kwon, Mun-Young | - |
dc.contributor.nonIdAuthor | Lee, Janghyun | - |
dc.contributor.nonIdAuthor | Kim, Kyeong Kyu | - |
dc.contributor.nonIdAuthor | Lee, Joon-Hwa | - |
dc.description.isOpenAccess | Y | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | Z-ALPHA DOMAIN | - |
dc.subject.keywordPlus | HANDED Z-DNA | - |
dc.subject.keywordPlus | NUCLEAR-MAGNETIC-RESONANCE | - |
dc.subject.keywordPlus | HUMAN EDITING ENZYME | - |
dc.subject.keywordPlus | MOLECULAR-CLONING | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | PROTON-EXCHANGE | - |
dc.subject.keywordPlus | HUMAN ADAR1 | - |
dc.subject.keywordPlus | NMR SYSTEM | - |
dc.subject.keywordPlus | CELLS | - |
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