Crystal Structure of the DNA Cytosine Deaminase APOBEC3F: The Catalytically Active and HIV-1 Vif-Binding Domain
Shandilya, Shivender M. D.
Albin, John S.
Anderson, Brett D.
McDougle, Rebecca M.
Carpenter, Michael A.
Davis, Ahkillah N.
Harris, Reuben S.
Schiffer, Celia A.
UMass Chan AffiliationsDepartment of Biochemistry and Molecular Pharmacology
Department of Pediatrics
vif Gene Products, Human Immunodeficiency Virus
Biochemistry, Biophysics, and Structural Biology
Immunology and Infectious Disease
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AbstractHuman 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.
SourceStructure. 2013 Jun 4;21(6):1042-50. doi: 10.1016/j.str.2013.04.010. Link to article on publisher's site
Permanent Link to this Itemhttp://hdl.handle.net/20.500.14038/29989
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