The current structural and functional understanding of APOBEC deaminases
- 23 June 2009
- journal article
- review article
- Published by Springer Science and Business Media LLC in Cellular and Molecular Life Sciences
- Vol. 66 (19), 3137-3147
- https://doi.org/10.1007/s00018-009-0070-y
Abstract
The apolipoprotein B mRNA-editing enzyme catalytic polypeptide (APOBEC) family of cytidine deaminases has emerged as an intensively studied field as a result of their important biological functions. These enzymes are involved in lipid metabolism, antibody diversification, and the inhibition of retrotransposons, retroviruses, and some DNA viruses. The APOBEC proteins function in these roles by deaminating single-stranded (ss) DNA or RNA. There are two high-resolution crystal structures available for the APOBEC family, Apo2 and the C-terminal catalytic domain (CD2) of Apo3G or Apo3G-CD2 [Holden et al. (Nature 456:121–124, 2008); Prochnow et al. (Nature 445:447–451, 2007)]. Additionally, the structure of Apo3G-CD2 has also been determined using NMR [Chen et al. (Nature 452:116–119, 2008); Furukawa et al. (EMBO J 28:440–451, 2009); Harjes et al. (J Mol Biol, 2009)]. A detailed structural analysis of the APOBEC proteins and a comparison to other zinc-coordinating deaminases can facilitate our understanding of how APOBEC proteins bind nucleic acids, recognize substrates, and form oligomers. Here, we review the recent development of structural and functional studies that apply to Apo3G as well as the APOBEC deaminase family.Keywords
This publication has 104 references indexed in Scilit:
- An Extended Structure of the APOBEC3G Catalytic Domain Suggests a Unique Holoenzyme ModelJournal of Molecular Biology, 2009
- Structure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3GThe EMBO Journal, 2009
- Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implicationsNature, 2008
- Functional domain organization of human APOBEC3GVirology, 2008
- Brca1 in immunoglobulin gene conversion and somatic hypermutationDNA Repair, 2008
- The intrinsic antiretroviral factor APOBEC3B contains two enzymatically active cytidine deaminase domainsVirology, 2007
- DNA Deamination in Immunity: AID in the Context of Its APOBEC RelativesAdvances in Immunology, 2007
- Cytidine Deamination of Retroviral DNA by Diverse APOBEC ProteinsCurrent Biology, 2004
- Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcriptsNature, 2003
- Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif proteinNature, 2002