Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration
| Autor: | Ying Huang, Ronglan Zheng, Mengli Cai, Myung Soo Lee, Robert Craigie, G. Marius Clore, Angela M. Gronenborn, Rodolfo Ghirlando, Shui-Qing Wei |
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| Rok vydání: | 1998 |
| Předmět: |
Models
Molecular Protein family Protein subunit Virus Integration Barrier-to-autointegration factor Molecular Sequence Data Helix-turn-helix Biology Crystallography X-Ray Biochemistry Protein Structure Secondary chemistry.chemical_compound Structural Biology Host chromosome Genetics Humans Amino Acid Sequence Peptide sequence Nuclear Magnetic Resonance Biomolecular Helix-Turn-Helix Motifs Sequence Homology Amino Acid Nuclear Proteins DNA DNA-Binding Proteins Crystallography Retroviridae chemistry DNA Viral Biophysics Nucleic Acid Conformation Dimerization |
| Zdroj: | Nature structural biology. 5(10) |
| ISSN: | 1072-8368 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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