HIV-1 Vif BC-box in Complex with Human ELOB and ELOC (PDB: 3DCG).[1]
Identifiers
Symbol
Vif
Pfam
PF00559
InterPro
IPR000475
Available protein structures:
Pfam
structures / ECOD
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
Viral infectivity factor, or Vif, is an accessory protein found in HIV and other lentiviruses. Its role is to disrupt the antiviral activity of the human enzyme APOBEC (specifically APOBEC3G, "A3G" in short, and other A3 enzymes) by targeting it for ubiquitination and cellular degradation. APOBEC is a cytidine deaminase enzyme that mutates viral nucleic acids.
Despite the functional and (weak) structural similarities, Vif found in lentiviruses can function in quite different ways. For example, the HIV-1 Vif ("Vif1" hereafter) and HIV-2 Vif ("Vif2") attach to APOBEC from different ends of themselves and have a different spectrum of inhibition. As HIV-1 is older and more virulent, many more studies have been done on the Vif1 than on the Vif2. Similarly, more studies have been done on the HIV/SIV Vif than on any other lentiviral Vif.[2]
^Cite error: The named reference pmid18562529 was invoked but never defined (see the help page).
^Smith, JL; Izumi, T; Borbet, TC; Hagedorn, AN; Pathak, VK (1 September 2014). "HIV-1 and HIV-2 Vif interact with human APOBEC3 proteins using completely different determinants". Journal of Virology. 88 (17): 9893–908. doi:10.1128/JVI.01318-14. PMC 4136346. PMID 24942576.
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