The current structural and functional understanding of APOBEC deaminases

@article{Bransteitter2009TheCS,
  title={The current structural and functional understanding of APOBEC deaminases},
  author={Ronda Bransteitter and Courtney Prochnow and Xiaojiang S. Chen},
  journal={Cellular and Molecular Life Sciences},
  year={2009},
  volume={66},
  pages={3137-3147}
}
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… Expand
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TLDR
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The structural and biochemical insights described here suggest that unique structural features on CD1 regulate the molecular assembly and catalytic activity of A3B through distinct mechanisms. Expand
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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References

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TLDR
The crystal structure of APO2 is reported and it is shown that AID deamination activity is impaired by mutations predicted to interfere with oligomerization and substrate access, resulting in defective antibody maturation. Expand
Antiviral Function of APOBEC3G Can Be Dissociated from Cytidine Deaminase Activity
TLDR
It is proposed that APOBEC3G can achieve an anti-HIV-1 effect through an undescribed mechanism that is distinct from cytidine deamination, and this findings reveal the nonequivalency of APOBec3G's N- and C-terminal domains and imply thatAPOB EC3G-mediated DNA editing may not always be necessary for antiviral activity. Expand
Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications
TLDR
The high-resolution crystal structure of the carboxy-terminal deaminase domain of APOBEC3G (APOBec3G-CD2) purified from Escherichia coli is reported, and residues involved in substrate specificity, single-stranded DNA binding and deaminases activity are identified. Expand
Dissecting APOBEC3G Substrate Specificity by Nucleoside Analog Interference*
TLDR
Nucleoside analog interference mapping is used to probe A3G-DNA interactions throughout the enzyme-substrate complex as well as to determine which DNA structural features determine substrate specificity, indicating that multiple components of nucleosides within the consensus sequence are important for substrate recognition by A2G, whereas deamination interference by analog substitution outside this region is minimal. Expand
Model Structure of Human APOBEC3G
TLDR
The structure model identifies a cluster of residues important for packaging of APOBEC3G into virions, and may serve to guide functional analysis ofAPOBEC2, which has no 3-D structure. Expand
Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G
TLDR
The structure of the APOBEC3G catalytic domain will help to understand functions of other family members and interactions that occur with pathogenic proteins such as HIV-1 Vif and Escherichia coli-based activity assays. Expand
An extended structure of the APOBEC3G catalytic domain suggests a unique holoenzyme model.
TLDR
This work compares the DNA cytidine deaminase activities and NMR structures of two A3G catalytic domain constructs and reveals part of the N-terminal pseudo-catalytic domain, including the interdomain linker and some of the last alpha-helix of the longer structure. Expand
The intrinsic antiretroviral factor APOBEC3B contains two enzymatically active cytidine deaminase domains.
TLDR
Enzymatically inactive mutant forms of APOBEC3G and APOBec3B were found to retain the ability to inhibit the infectivity of HIV-1 virions produced in their presence by approximately 4-fold and approximately 8-fold, respectively. Expand
DNA deamination in immunity: AID in the context of its APOBEC relatives.
TLDR
It is proposed that the cytosine and tRNA deaminases are likely to provide better structural paradigms for the AID/APOBEC family than do the cytidine deamin enzymes, to which they have conventionally been compared. Expand
APOBEC3F Can Inhibit the Accumulation of HIV-1 Reverse Transcription Products in the Absence of Hypermutation
TLDR
Data suggest that both APOBEC3F and APOB EC3G are able to function as antiviral factors in the absence of cytidine deamination, that this editing-independent activity is an important aspect of APOBec protein-mediated antiviral phenotypes, but that APOBE3F may be a better model in which to study it. Expand
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