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- W2005890610 abstract "Human APOBEC3F is an antiretroviral single-strand DNA cytosine deaminase, susceptible to degradation by the HIV-1 protein Vif. In this study the crystal structure of the HIV Vif binding, catalytically active, C-terminal domain of APOBEC3F (A3F-CTD) was determined. The A3F-CTD shares structural motifs with portions of APOBEC3G-CTD, APOBEC3C, and APOBEC2. Residues identified to be critical for Vif-dependent degradation of APOBEC3F all fit within a predominantly negatively charged contiguous region on the surface of A3F-CTD. Specific sequence motifs, previously shown to play a role in Vif susceptibility and virion encapsidation, are conserved across APOBEC3s and between APOBEC3s and HIV-1 Vif. In this structure these motifs pack against each other at intermolecular interfaces, providing potential insights both into APOBEC3 oligomerization and Vif interactions." @default.
- W2005890610 created "2016-06-24" @default.
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- W2005890610 date "2013-06-01" @default.
- W2005890610 modified "2023-10-10" @default.
- W2005890610 title "Crystal Structure of the DNA Cytosine Deaminase APOBEC3F: The Catalytically Active and HIV-1 Vif-Binding Domain" @default.
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- W2005890610 doi "https://doi.org/10.1016/j.str.2013.04.010" @default.
- W2005890610 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3805256" @default.
- W2005890610 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23685212" @default.
- W2005890610 hasPublicationYear "2013" @default.
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