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Structural basis for stable DNA complex formation by the caspase-activated DNase

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dc.contributor.author Reh S.
dc.contributor.author Korn C.
dc.contributor.author Gimadutdinow O.
dc.contributor.author Meiss G.
dc.date.accessioned 2018-09-17T20:20:51Z
dc.date.available 2018-09-17T20:20:51Z
dc.date.issued 2005
dc.identifier.issn 0021-9258
dc.identifier.uri https://dspace.kpfu.ru/xmlui/handle/net/133374
dc.description.abstract We describe a structural model for DNA binding by the caspase-activated DNase (CAD). Results of a mutational analysis and computational modeling suggest that DNA is bound via a positively charged surface with two functionally distinct regions, one being the active site facing the DNA minor groove and the other comprising distal residues close to or directly from helix α4, which binds DNA in the major groove. This bipartite protein-DNA interaction is present once in the CAD/inhibitor of CAD heterodimer and repeated twice in the active CAD dimer. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
dc.relation.ispartofseries Journal of Biological Chemistry
dc.title Structural basis for stable DNA complex formation by the caspase-activated DNase
dc.type Article
dc.relation.ispartofseries-issue 50
dc.relation.ispartofseries-volume 280
dc.collection Публикации сотрудников КФУ
dc.relation.startpage 41707
dc.source.id SCOPUS00219258-2005-280-50-SID29244462831


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  • Публикации сотрудников КФУ Scopus [24551]
    Коллекция содержит публикации сотрудников Казанского федерального (до 2010 года Казанского государственного) университета, проиндексированные в БД Scopus, начиная с 1970г.

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