ArticleProceedings of the National Academy of Sciences of the United States of America2009
Model structure of APOBEC3C reveals a binding pocket modulating ribonucleic acid interaction required for encapsidation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.
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Who cites it
21 citing papers in PubMed, 1 synthesis or guideline pooled it, 41 citations in OpenAlex.
- HIV Genome-Wide Protein Associations: a Review of 30 Years of Research.Microbiology and molecular biology reviews : MMBR · 2016Pooled it
- Mechanisms of APOBEC3 Packaging into HIV-1.Viruses · 2026Review
- Review
- Deamination hotspots among APOBEC3 family members are defined by both target site sequence context and ssDNA secondary structure.Nucleic acids research · 2020Article
- Off-target RNA mutation induced by DNA base editing and its elimination by mutagenesis.Nature · 2019Article
- Review
- Cytidine deaminase efficiency of the lentiviral viral restriction factor APOBEC3C correlates with dimerization.Nucleic acids research · 2017Article
- The ClusPro web server for protein-protein docking.Nature protocols · 2017Article
- Vif Proteins from Diverse Human Immunodeficiency Virus/Simian Immunodeficiency Virus Lineages Have Distinct Binding Sites in A3C.Journal of virology · 2016Article
- The RNA Binding Specificity of Human APOBEC3 Proteins Resembles That of HIV-1 Nucleocapsid.PLoS pathogens · 2016Article
- A computational analysis of the structural determinants of APOBEC3's catalytic activity and vulnerability to HIV-1 Vif.Virology · 2014Article
- APOBEC3 multimerization correlates with HIV-1 packaging and restriction activity in living cells.Journal of molecular biology · 2014Article
- Human LINE-1 restriction by APOBEC3C is deaminase independent and mediated by an ORF1p interaction that affects LINE reverse transcriptase activity.Nucleic acids research · 2014Article
- The APOBEC3C crystal structure and the interface for HIV-1 Vif binding.Nature structural & molecular biology · 2012Article
- Functions and regulation of the APOBEC family of proteins.Seminars in cell & developmental biology · 2012Review
- Structure-based systems biology for analyzing off-target binding.Current opinion in structural biology · 2011Review
- Structure-function analyses point to a polynucleotide-accommodating groove essential for APOBEC3A restriction activities.Journal of virology · 2011Article
- The chemical basis of pharmacology.Biochemistry · 2010Review
- Binding of protein kinase inhibitors to synapsin I inferred from pair-wise binding site similarity measurements.PloS one · 2010Article
- Rationalisation of the differences between APOBEC3G structures from crystallography and NMR studies by molecular dynamics simulations.PloS one · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human APOBEC3 (A3) proteins form part of the intrinsic immunity to retroviruses. Carrying 1 or 2 copies of a cytidine deaminase motif, A3s act by deamination of retroviral genomes during reverse transcription. HIV-1 overcomes this inhibition by the Vif protein, which prevents incorporation of A3 into virions. In this study we modeled and probed the structure of APOBEC3C (A3C), a single-domain A3 with strong antilentiviral activity. The 3-dimensional protein model was used to predict the effect of mutations on antiviral activity, which was tested in a Deltavif simian immunodeficiency virus (SIV) reporter virus assay. We found that A3C activity requires protein dimerization for antiviral activity against SIV. Furthermore, by using a structure-based algorithm for automated pocket extraction, we detected a putative substrate binding pocket of A3C distal from the zinc-coordinating deaminase motif. Mutations in this region diminished antiviral activity by excluding A3C from virions. We found evidence that the small 5.8S RNA specifically binds to this locus and mediates incorporation of A3C into virus particles.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.