ArticleVirology2014
A computational analysis of the structural determinants of APOBEC3's catalytic activity and vulnerability to HIV-1 Vif.
Article in Virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 26 citations in OpenAlex.
- Review
- Article
- APOBEC3B drives PKR-mediated translation shutdown and protects stress granules in response to viral infection.Nature communications · 2023Article
- Exploring ABOBEC3A and APOBEC3B substrate specificity and their role in HPV positive head and neck cancer.iScience · 2022Article
- Characterization of an A3G-VifMolecular & cellular proteomics : MCP · 2021Article
- Polymorphisms in Human APOBEC3H Differentially Regulate Ubiquitination and Antiviral Activity.Viruses · 2020Article
- Deamination hotspots among APOBEC3 family members are defined by both target site sequence context and ssDNA secondary structure.Nucleic acids research · 2020Article
- Article
- Site- and degree-specific C-H oxidation on 5-methylcytosine homologues for probing active DNA demethylation.Chemical science · 2019Article
- Determinants of Oligonucleotide Selectivity of APOBEC3B.Journal of chemical information and modeling · 2019Article
- Pan-cancer transcriptomic analysis dissects immune and proliferative functions of APOBEC3 cytidine deaminases.Nucleic acids research · 2019Article
- Conformational Switch Regulates the DNA Cytosine Deaminase Activity of Human APOBEC3B.Scientific reports · 2017Article
- Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificity.Nature communications · 2017Article
- Crystal structures of APOBEC3G N-domain alone and its complex with DNA.Nature communications · 2016Article
- 1.92 Angstrom Zinc-Free APOBEC3F Catalytic Domain Crystal Structure.Journal of molecular biology · 2016Article
- Nuclear Magnetic Resonance Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity.Biochemistry · 2016Article
- Inhibition of APOBEC3G activity impedes double-stranded DNA repair.The FEBS journal · 2016Article
- Zinc enhancement of cytidine deaminase activity highlights a potential allosteric role of loop-3 in regulating APOBEC3 enzymes.Scientific reports · 2015Article
- Natural Polymorphisms and Oligomerization of Human APOBEC3H Contribute to Single-stranded DNA Scanning Ability.The Journal of biological chemistry · 2015Article
- Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G.Nature structural & molecular biology · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
APOBEC3s (A3) are Zn(2+) dependent cytidine deaminases with diverse biological functions and implications for cancer and immunity. Four of the seven human A3s restrict HIV by 'hypermutating' the reverse-transcribed viral genomic DNA. HIV Virion Infectivity Factor (Vif) counters this restriction by targeting A3s to proteasomal degradation. However, there is no apparent correlation between catalytic activity, Vif binding, and sequence similarity between A3 domains. Our comparative structural analysis reveals features required for binding Vif and features influencing polynucleotide deaminase activity in A3 proteins. All Vif-binding A3s share a negatively charged surface region that includes residues previously implicated in binding the highly-positively charged Vif. Additionally, catalytically active A3s share a positively charged groove near the Zn(2+) coordinating active site, which may accommodate the negatively charged polynucleotide substrate. Our findings suggest surface electrostatics, as well as the spatial extent of substrate accommodating region, are critical determinants of substrate and Vif binding across A3 proteins with implications for anti-retroviral and anti-cancer therapeutic design.
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