ArticleBiochemistry2012
APOBEC2 is a monomer in solution: implications for APOBEC3G models.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 31 citations in OpenAlex.
- APOBEC2 safeguards skeletal muscle cell fate through binding chromatin and regulating transcription of non-muscle genes during myoblast differentiation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Functions and consequences of AID/APOBEC-mediated DNA and RNA deamination.Nature reviews. Genetics · 2022Review
- Structure-Based Design of First-Generation Small Molecule Inhibitors Targeting the Catalytic Pockets of AID, APOBEC3A, and APOBEC3B.ACS pharmacology & translational science · 2021Article
- Review
- The Role of APOBECs in Viral Replication.Microorganisms · 2020Review
- An Insulin-Responsive Sensor in the SIRT1 Disordered Region Binds DBC1 and PACS-2 to Control Enzyme Activity.Molecular cell · 2018Article
- Modeling the Embrace of a Mutator: APOBEC Selection of Nucleic Acid Ligands.Trends in biochemical sciences · 2018Review
- Apobec2 deficiency causes mitochondrial defects and mitophagy in skeletal muscle.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Article
- Review
- A Novel Regulator of Activation-Induced Cytidine Deaminase/APOBECs in Immunity and Cancer: Schrödinger's CATalytic Pocket.Frontiers in immunology · 2017Review
- Structural and functional assessment of APOBEC3G macromolecular complexes.Methods (San Diego, Calif.) · 2016Article
- The APOBEC Protein Family: United by Structure, Divergent in Function.Trends in biochemical sciences · 2016Review
- Functional requirements of AID's higher order structures and their interaction with RNA-binding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Crystal Structure of the DNA Deaminase APOBEC3B Catalytic Domain.The Journal of biological chemistry · 2015Article
- Natural Polymorphisms and Oligomerization of Human APOBEC3H Contribute to Single-stranded DNA Scanning Ability.The Journal of biological chemistry · 2015Article
- Zinc-binding domain-dependent, deaminase-independent actions of apolipoprotein B mRNA-editing enzyme, catalytic polypeptide 2 (Apobec2), mediate its effect on zebrafish retina regeneration.The Journal of biological chemistry · 2014Article
- APOBEC3 multimerization correlates with HIV-1 packaging and restriction activity in living cells.Journal of molecular biology · 2014Article
- Multiple APOBEC3 restriction factors for HIV-1 and one Vif to rule them all.Journal of molecular biology · 2014Review
- Binding of RNA by APOBEC3G controls deamination-independent restriction of retroviruses.Nucleic acids research · 2013Article
- NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity.Nature communications · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Although the physiological role of APOBEC2 is still largely unknown, a crystal structure of a truncated variant of this protein was determined several years ago [Prochnow, C. (2007) Nature445, 447-451]. This APOBEC2 structure had considerable impact in the HIV field because it was considered a good model for the structure of APOBEC3G, an important HIV restriction factor that abrogates HIV infectivity in the absence of the viral accessory protein Vif. The quaternary structure and the arrangement of the monomers of APOBEC2 in the crystal were taken as being representative for APOBEC3G and exploited in explaining its enzymatic and anti-HIV activity. Here we show, unambiguously, that in contrast to the findings for the crystal, APOBEC2 is monomeric in solution. The nuclear magnetic resonance solution structure of full-length APOBEC2 reveals that the N-terminal tail that was removed for crystallization resides close to strand β2, the dimer interface in the crystal structure, and shields this region of the protein from engaging in intermolecular contacts. In addition, the presence of the N-terminal region drastically alters the aggregation propensity of APOBEC2, rendering the full-length protein highly soluble and not prone to precipitation. In summary, our results cast doubt on all previous structure-function predictions for APOBEC3G that were based on the crystal structure of APOBEC2.
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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.