This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2bzf
From Proteopedia
STRUCTURAL BASIS FOR DNA BRIDGING BY BARRIER-TO-AUTOINTEGRATION FACTOR (BAF)
Overview
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.
About this Structure
2BZF is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for DNA bridging by barrier-to-autointegration factor., Bradley CM, Ronning DR, Ghirlando R, Craigie R, Dyda F, Nat Struct Mol Biol. 2005 Oct;12(10):935-6. Epub 2005 Sep 11. PMID:16155580 Page seeded by OCA on Sat May 3 21:00:49 2008
