Article
Importance of the proline-rich multimerization domain on the oligomerization and nucleic acid binding properties of HIV-1 Vif.
Nucleic acids research - 1 Mar 2011
Bernacchi Serena, Mercenne Gaëlle, Tournaire Clémence, Marquet Roland, Paillart Jean-Christophe
Abstract excerpt
The HIV-1 viral infectivity factor (Vif) is required for productive infection of non-permissive cells, including most natural HIV-1 targets, where it counteracts the antiviral activities of the cellular cytosine deaminases APOBEC-3G (A3G) and A3F. Vif is a multimeric protein and the conserved proline-rich domain (161)PPLP(164) regulating Vif oligomerization is crucial for its function and viral infectivity. Here,...
Topics
- Amino Acid Motifs
- Amino Acid Substitution
- Fluorescence
- HIV-1
- Mutation
- Proline
- Protein Binding
- Protein Folding
- Protein Multimerization
- Protein Structure, Secondary
- Protein Structure, Tertiary
- RNA, Viral
- RNA-Binding Proteins
- vif Gene Products, Human Immunodeficiency Virus