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Core-binding factor β increases the affinity between human Cullin 5 and HIV-1 Vif within an E3 ligase complex.

Biochemistry | Nov 6, 2012

http://www.ncbi.nlm.nih.gov/pubmed/23098073

HIV-1 Vif masquerades as a receptor for a cellular E3 ligase harboring Elongin B, Elongin C, and Cullin 5 (EloB/C/Cul5) proteins that facilitate degradation of the antiretroviral factor APOBEC3G (A3G). This Vif-mediated activity requires human core-binding factor β (CBFβ) in contrast to cellular substrate receptors. We observed calorimetrically that Cul5 binds tighter to full-length Vif((1-192))/EloB/C/CBFβ (K(d) = 5 ± 2 nM) than to Vif((95-192))/EloB/C (K(d) = 327 ± 40 nM), which cannot bind CBFβ. A comparison of heat capacity changes supports a model in which CBFβ prestabilizes Vif((1-192)) relative to Vif((95-192)), consistent with a stronger interaction of Cul5 with Vif's C-terminal Zn(2+)-binding motif. An additional interface between Cul5 and an N-terminal region of Vif appears to be plausible, which has therapeutic design implications.

Pubmed ID: 23098073 RIS Download

Mesh terms: Core Binding Factor beta Subunit | Cullin Proteins | Humans | Thermodynamics | Ubiquitin-Protein Ligases | vif Gene Products, Human Immunodeficiency Virus

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Associated grants

  • Agency: NIAID NIH HHS, Id: R33 AI076085
  • Agency: NIAID NIH HHS, Id: R33 AI076085

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