Structural basis for DNA bridging by barrier-to-autointegration factor

Nat Struct Mol Biol. 2005 Oct;12(10):935-6. doi: 10.1038/nsmb989. Epub 2005 Sep 11.


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.

Publication types

  • Research Support, N.I.H., Intramural

MeSH terms

  • Amino Acid Sequence
  • Crystallography
  • DNA / chemistry*
  • DNA / metabolism
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / metabolism
  • Helix-Loop-Helix Motifs
  • Humans
  • Molecular Sequence Data
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / metabolism
  • Protein Conformation


  • BANF1 protein, human
  • DNA-Binding Proteins
  • Nuclear Proteins
  • DNA

Associated data

  • PDB/2BZF