2EZX

SOLUTION STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR BAF, NMR, REGULARIZED MEAN STRUCTURE

Summary for 2EZX

• Entry DOI: 10.2210/pdb2ezx/pdb
• Descriptor: BARRIER-TO-AUTOINTEGRATION FACTOR (1 entity in total)
• Functional Keywords: dna-binding protein, integration, aids, retroviruses, dna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: O75531
• Total number of polymer chains: 2
• Total formula weight: 20147.18

Authors

Clore, G.M.,Cai, M.,Gronenborn, A.M. (deposition date: 1998-07-26, release date: 1999-01-13, Last modification date: 2024-05-29)

Primary citation

Cai, M.,Huang, Y.,Zheng, R.,Wei, S.Q.,Ghirlando, R.,Lee, M.S.,Craigie, R.,Gronenborn, A.M.,Clore, G.M.
Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration.
Nat.Struct.Biol., 5:903-909, 1998

PubMed Abstract: The solution structure of the human barrier-to-autointegration factor, BAF, a 21,000 Mr dimer, has been solved by NMR, including extensive use of dipolar couplings which provide a priori long range structural information. BAF is a highly evolutionarily conserved DNA binding protein that is responsible for inhibiting autointegration of retroviral DNA, thereby promoting integration of retroviral DNA into the host chromosome. BAF is largely helical, and each subunit is composed of five helices. The dimer is elongated in shape and the dimer interface comprises principally hydrophobic contacts supplemented by a single salt bridge. Despite the absence of any sequence similarity to any other known protein family, the topology of helices 3-5 is similar to that of a number of DNA binding proteins, with helices 4 and 5 constituting a helix-turn-helix motif. A model for the interaction of BAF with DNA that is consistent with structural and mutagenesis data is proposed.

PubMed: 9783751
DOI: 10.1038/2345

Experimental method

SOLUTION NMR