Bohn, Markus-FrederikShandilya, Shivender M. D.Albin, John S.Kouno, TakahideAnderson, Brett D.McDougle, Rebecca M.Carpenter, Michael A.Rathore, AnuragEvans, LeahDavis, Ahkillah N.Zhang, JingYingLu, YongjianSomasundaran, MohanMatsuo, HiroshiHarris, Reuben S.Schiffer, Celia A.2022-08-232022-08-232013-06-042013-06-05Structure. 2013 Jun 4;21(6):1042-50. doi: 10.1016/j.str.2013.04.010. <a href="http://dx.doi.org/10.1016/j.str.2013.04.010" target="_blank">Link to article on publisher's site</a>0969-2126 (Linking)10.1016/j.str.2013.04.01023685212https://hdl.handle.net/20.500.14038/29989Human 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.en-USCytosine Deaminasevif Gene Products, Human Immunodeficiency VirusBiochemistry, Biophysics, and Structural BiologyImmunology and Infectious DiseaseJournal Articlehttps://escholarship.umassmed.edu/faculty_pubs/224199952faculty_pubs/22