Abstract:
:The ability of barrier-to-autointegration factor (BAF) to bind and bridge DNA in a sequence-independent manner is crucial for its role in retroviral integration and a variety of cellular processes. To better understand this behavior, we solved the crystal structure of BAF bound to DNA. The structure reveals that BAF bridges DNA using two pairs of helix-hairpin-helix motifs located on opposite surfaces of the BAF dimer without changing its conformation.
journal_name
Nat Struct Mol Bioljournal_title
Nature structural & molecular biologyauthors
Bradley CM,Ronning DR,Ghirlando R,Craigie R,Dyda Fdoi
10.1038/nsmb989keywords:
subject
Has Abstractpub_date
2005-10-01 00:00:00pages
935-6issue
10eissn
1545-9993issn
1545-9985pii
nsmb989journal_volume
12pub_type
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