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    Crystal Structure of the DNA Cytosine Deaminase APOBEC3F: The Catalytically Active and HIV-1 Vif-Binding Domain

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    Authors
    Bohn, Markus-Frederik
    Shandilya, 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.
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    UMass Chan Affiliations
    Department of Biochemistry and Molecular Pharmacology
    Department of Pediatrics
    Document Type
    Journal Article
    Publication Date
    2013-06-04
    Keywords
    Cytosine Deaminase
    vif Gene Products, Human Immunodeficiency Virus
    Biochemistry, Biophysics, and Structural Biology
    Immunology and Infectious Disease
    
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    Link to Full Text
    http://dx.doi.org/10.1016/j.str.2013.04.010
    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.
    Source
    Structure. 2013 Jun 4;21(6):1042-50. doi: 10.1016/j.str.2013.04.010. Link to article on publisher's site
    DOI
    10.1016/j.str.2013.04.010
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/29989
    PubMed ID
    23685212
    Related Resources
    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.str.2013.04.010
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