DSpace at KISTKIST Article2010

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dc.contributor.authorSeo, Yeo-Jin-
dc.contributor.authorAhn, Hee-Chul-
dc.contributor.authorLee, Eun-Hae-
dc.contributor.authorBang, Jongchul-
dc.contributor.authorKang, Young-Min-
dc.contributor.authorKim, Hee-Eun-
dc.contributor.authorLee, Yeon-Mi-
dc.contributor.authorKim, Kyungmin-
dc.contributor.authorChoi, Byong-Seok-
dc.contributor.authorLee, Joon-Hwa-
dc.date.accessioned2024-01-20T18:30:55Z-
dc.date.available2024-01-20T18:30:55Z-
dc.date.created2021-09-05-
dc.date.issued2010-10-22-
dc.identifier.issn0014-5793-
dc.identifier.urihttps://pubs.kist.re.kr/handle/201004/130992-
dc.description.abstractThe Z alpha domain of human ADAR1 (Z alpha(ADAR1)) preferentially binds Z-DNA rather than B-DNA with high binding affinity. Z alpha(ADAR1) binds to the Z-conformation of both non-CG-repeat DNA duplexes and a d(CGCGCG)(2) duplex similarly. We performed NMR experiments on complexes between the Z alpha(ADAR1) and non-CG-repeat DNA duplexes, d(CACGTG)(2) or d(CGTACG)(2), with a variety of protein-DNA molar ratios. Comparison of these results with those from the analysis of d(CGCGCG)(2) in the previous study suggests that Za(ADAR1) exhibits the sequence preference of d(CGCGCG)(2) >> d(CACGTG)(2) > d(CGTACG)(2) through multiple sequence discrimination steps during the B-Z transition. (C)2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.-
dc.languageEnglish-
dc.publisherWILEY-
dc.subjectHANDED Z-DNA-
dc.subjectHUMAN EDITING ENZYME-
dc.subjectCRYSTAL-STRUCTURE-
dc.subjectBINDING DOMAIN-
dc.subjectBASE-PAIRS-
dc.subjectPROTON-EXCHANGE-
dc.subjectREVEALS-
dc.subjectKINETICS-
dc.subjectCOMPLEX-
dc.subjectTHERMODYNAMICS-
dc.titleSequence discrimination of the Z alpha domain of human ADAR1 during B-Z transition of DNA duplexes-
dc.typeArticle-
dc.identifier.doi10.1016/j.febslet.2010.09.036-
dc.description.journalClass1-
dc.identifier.bibliographicCitationFEBS LETTERS, v.584, no.20, pp.4344 - 4350-
dc.citation.titleFEBS LETTERS-
dc.citation.volume584-
dc.citation.number20-
dc.citation.startPage4344-
dc.citation.endPage4350-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.identifier.wosid000283060100013-
dc.identifier.scopusid2-s2.0-77957793667-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryBiophysics-
dc.relation.journalWebOfScienceCategoryCell Biology-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaBiophysics-
dc.relation.journalResearchAreaCell Biology-
dc.type.docTypeArticle-
dc.subject.keywordPlusHANDED Z-DNA-
dc.subject.keywordPlusHUMAN EDITING ENZYME-
dc.subject.keywordPlusCRYSTAL-STRUCTURE-
dc.subject.keywordPlusBINDING DOMAIN-
dc.subject.keywordPlusBASE-PAIRS-
dc.subject.keywordPlusPROTON-EXCHANGE-
dc.subject.keywordPlusREVEALS-
dc.subject.keywordPlusKINETICS-
dc.subject.keywordPlusCOMPLEX-
dc.subject.keywordPlusTHERMODYNAMICS-
dc.subject.keywordAuthorNMR-
dc.subject.keywordAuthorZ-DNA-
dc.subject.keywordAuthorHydrogen exchange-
dc.subject.keywordAuthorZ-DNA binding protein-
dc.subject.keywordAuthorB-Z transition-
dc.subject.keywordAuthorNon-CG repeat DNA-
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