ArticleACS central science2017
Computational Model and Dynamics of Monomeric Full-Length APOBEC3G.
Article in ACS central science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Article
- Structural insights into RNA bridging between HIV-1 Vif and antiviral factor APOBEC3G.Nature communications · 2023Article
- Antiretroviral APOBEC3 cytidine deaminases alter HIV-1 provirus integration site profiles.Nature communications · 2023Article
- Exploring ABOBEC3A and APOBEC3B substrate specificity and their role in HPV positive head and neck cancer.iScience · 2022Article
- Review
- Characterization of an A3G-VifMolecular & cellular proteomics : MCP · 2021Article
- Atomic Force Microscopy Reveals that the Drosophila Telomere-Capping Protein Verrocchio Is a Single-Stranded DNA-Binding Protein.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Crystal Structure of a Soluble APOBEC3G Variant Suggests ssDNA to Bind in a Channel that Extends between the Two Domains.Journal of molecular biology · 2020Article
- High-speed atomic force microscopy directly visualizes conformational dynamics of the HIV Vif protein in complex with three host proteins.The Journal of biological chemistry · 2020Article
- Occurrence and stability of lone pair-π and OH-π interactions between water and nucleobases in functional RNAs.Nucleic acids research · 2020Article
- Understanding the structural basis of HIV-1 restriction by the full length double-domain APOBEC3G.Nature communications · 2020Article
- Article
- Insight into dynamics of APOBEC3G protein in complexes with DNA assessed by high speed AFM.Nanoscale advances · 2019Article
- Structural Determinants of the APOBEC3G N-Terminal Domain for HIV-1 RNA Association.Frontiers in cellular and infection microbiology · 2019Article
- The Enzymatic Activity of APOBE3G Multimers.Scientific reports · 2018Article
- Modeling the Embrace of a Mutator: APOBEC Selection of Nucleic Acid Ligands.Trends in biochemical sciences · 2018Review
- Direct AFM Visualization of the Nanoscale Dynamics of Biomolecular Complexes.Journal of physics D: Applied physics · 2018Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
APOBEC3G (A3G) is a restriction factor that provides innate immunity against HIV-1 in the absence of viral infectivity factor (Vif) protein. However, structural information about A3G, which can aid in unraveling the mechanisms that govern its interactions and define its antiviral activity, remains unknown. Here, we built a computer model of a full-length A3G using docking approaches and molecular dynamics simulations, based on the available X-ray and NMR structural data for the two protein domains. The model revealed a large-scale dynamics of the A3G monomer, as the two A3G domains can assume compact forms or extended dumbbell type forms with domains visibly separated from each other. To validate the A3G model, we performed time-lapse high-speed atomic force microscopy (HS-AFM) experiments enabling us to get images of a fully hydrated A3G and to directly visualize its dynamics. HS-AFM confirmed that A3G exists in two forms, a globular form (∼84% of the time) and a dumbbell form (∼16% of the time), and can dynamically switch from one form to the other. The obtained HS-AFM results are in line with the computer modeling, which demonstrates a similar distribution between two forms. Furthermore, our simulations capture the complete process of A3G switching from the DNA-bound state to the closed state. The revealed dynamic nature of monomeric A3G could aid in target recognition including scanning for cytosine locations along the DNA strand and in interactions with viral RNA during packaging into HIV-1 particles.
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Registered trials
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.