Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 12, Issue 10, Pages 935-936Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb989
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Funding
- Intramural NIH HHS Funding Source: Medline
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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.
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