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.
Original language | English (US) |
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Pages (from-to) | 935-936 |
Number of pages | 2 |
Journal | Nature Structural and Molecular Biology |
Volume | 12 |
Issue number | 10 |
DOIs | |
State | Published - Oct 2005 |
Externally published | Yes |
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology