ArticleJournal of molecular biology2009
An extended structure of the APOBEC3G catalytic domain suggests a unique holoenzyme model.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.
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Who cites it
81 citing papers in PubMed, 103 citations in OpenAlex.
- Article
- The current toolbox for APOBEC drug discovery.Trends in pharmacological sciences · 2022Review
- Review
- Characterization of an A3G-VifMolecular & cellular proteomics : MCP · 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
- Review
- Article
- APOBEC3s: DNA-editing human cytidine deaminases.Protein science : a publication of the Protein Society · 2019Review
- Mechanism for APOBEC3G catalytic exclusion of RNA and non-substrate DNA.Nucleic acids research · 2019Article
- Structural Analysis of the Active Site and DNA Binding of Human Cytidine Deaminase APOBEC3B.Journal of chemical theory and computation · 2019Article
- Insight into dynamics of APOBEC3G protein in complexes with DNA assessed by high speed AFM.Nanoscale advances · 2019Article
- Modeling the Embrace of a Mutator: APOBEC Selection of Nucleic Acid Ligands.Trends in biochemical sciences · 2018Review
- Crystal structure of the catalytic domain of HIV-1 restriction factor APOBEC3G in complex with ssDNA.Nature communications · 2018Article
- Insights into DNA substrate selection by APOBEC3G from structural, biochemical, and functional studies.PloS one · 2018Article
- Direct AFM Visualization of the Nanoscale Dynamics of Biomolecular Complexes.Journal of physics D: Applied physics · 2018Article
- Computational Model and Dynamics of Monomeric Full-Length APOBEC3G.ACS central science · 2017Article
- Review
- Identification and characterization of loop7 motif and its role in regulating biological function of human APOBEC3G through molecular modeling and biological assay.Acta pharmaceutica Sinica. B · 2017Article
- Structural determinants of APOBEC3B non-catalytic domain for molecular assembly and catalytic regulation.Nucleic acids research · 2017Article
- NMR-based method of small changes reveals how DNA mutator APOBEC3A interacts with its single-stranded DNA substrate.Nucleic acids research · 2017Article
21 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Human APOBEC3G (A3G) belongs to a family of polynucleotide cytidine deaminases. This family includes APOBEC1 and AID, which edit APOB mRNA and antibody gene DNA, respectively. A3G deaminates cytidines to uridines in single-strand DNA and inhibits the replication of human immunodeficiency virus-1, other retroviruses, and retrotransposons. Although the mechanism of A3G-catalyzed DNA deamination has been investigated genetically and biochemically, atomic details are just starting to emerge. Here, we compare the DNA cytidine deaminase activities and NMR structures of two A3G catalytic domain constructs. The longer A3G191-384 protein is considerably more active than the shorter A3G198-384 variant. The longer structure has an alpha1-helix (residues 201-206) that was not apparent in the shorter protein, and it contributes to catalytic activity through interactions with hydrophobic core structures (beta1, beta3, alpha5, and alpha6). Both A3G catalytic domain solution structures have a discontinuous beta2 region that is clearly different from the continuous beta2 strand of another family member, APOBEC2. In addition, the longer A3G191-384 structure revealed part of the N-terminal pseudo-catalytic domain, including the interdomain linker and some of the last alpha-helix. These structured residues (residues 191-196) enabled a novel full-length A3G model by providing physical overlap between the N-terminal pseudo-catalytic domain and the new C-terminal catalytic domain structure. Contrary to predictions, this structurally constrained model suggested that the two domains are tethered by structured residues and that the N- and C-terminal beta2 regions are too distant from each other to participate in this interaction.
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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.