Crystal Structure of the DNA Cytosine Deaminase APOBEC3F: The Catalytically Active and HIV-1 Vif-Binding Domain
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Authors
Bohn, Markus-FrederikShandilya, Shivender M. D.
Albin, John S.
Kouno, Takahide
Anderson, Brett D.
McDougle, Rebecca M.
Carpenter, Michael A.
Rathore, Anurag
Evans, Leah
Davis, Ahkillah N.
Zhang, JingYing
Lu, Yongjian
Somasundaran, Mohan
Matsuo, Hiroshi
Harris, Reuben S.
Schiffer, Celia A.
UMass Chan Affiliations
Department of Biochemistry and Molecular PharmacologyDepartment of Pediatrics
Document Type
Journal ArticlePublication Date
2013-06-04Keywords
Cytosine Deaminasevif Gene Products, Human Immunodeficiency Virus
Biochemistry, Biophysics, and Structural Biology
Immunology and Infectious Disease
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Show full item recordAbstract
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.Source
Structure. 2013 Jun 4;21(6):1042-50. doi: 10.1016/j.str.2013.04.010. Link to article on publisher's siteDOI
10.1016/j.str.2013.04.010Permanent Link to this Item
http://hdl.handle.net/20.500.14038/29989PubMed ID
23685212Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1016/j.str.2013.04.010