The APOBEC-2 crystal structure and functional implications for the deaminase AID

@article{Prochnow2007TheAC,
  title={The APOBEC-2 crystal structure and functional implications for the deaminase AID},
  author={Courtney Prochnow and R. Bransteitter and M. Klein and M. Goodman and Xiaojiang S. Chen},
  journal={Nature},
  year={2007},
  volume={445},
  pages={447-451}
}
APOBEC-2 (APO2) belongs to the family of apolipoprotein B messenger RNA-editing enzyme catalytic (APOBEC) polypeptides, which deaminates mRNA and single-stranded DNA. Different APOBEC members use the same deamination activity to achieve diverse human biological functions. Deamination by an APOBEC protein called activation-induced cytidine deaminase (AID) is critical for generating high-affinity antibodies, and deamination by APOBEC-3 proteins can inhibit retrotransposons and the replication of… Expand
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References

SHOWING 1-10 OF 34 REFERENCES
Monomeric APOBEC3G Is Catalytically Active and Has Antiviral Activity
TLDR
It is found that human APO3G is capable of forming multimeric complexes in transfected HeLa cells and an important role for C97 in the RNA-dependent multimerization of this protein is demonstrated. Expand
Evolution of the AID/APOBEC family of polynucleotide (deoxy)cytidine deaminases.
TLDR
It is found that although the family forms part of a larger superfamily of deaminases distributed throughout the biological world, the AID/APOBEC family itself is restricted to vertebrates with homologs of AID (a DNA deaminase that triggers antibody gene diversification) and of APOBEC2 (unknown function) identifiable in sequence databases from bony fish, birds, amphibians, and mammals. Expand
The structure of a yeast RNA-editing deaminase provides insight into the fold and function of activation-induced deaminase and APOBEC-1.
TLDR
The results suggested both AID and APOBEC-1 are equally likely to bind single-stranded DNA or RNA, which has implications for the identification of natural AID targets. Expand
Complementary function of the two catalytic domains of APOBEC3G.
TLDR
A model in which CD1 mediates encapsidation and RNA binding while CD2 mediates cytidine deaminase activity is suggested, which suggests that HTLV-I was relatively resistant to the antiviral effects of encapsidated APOBEC3G. Expand
APOBEC deaminases as cellular antiviral factors: a novel natural host defense mechanism.
  • R. Franca, S. Spadari, G. Maga
  • Biology, Medicine
  • Medical science monitor : international medical journal of experimental and clinical research
  • 2006
TLDR
This article is aimed at broadening the current knowledge about the antiviral activity of the APOBEC members and to highlight the notion that their role(s) might be more general than previously anticipated. Expand
ARCD-1, an apobec-1-related cytidine deaminase, exerts a dominant negative effect on C to U RNA editing.
TLDR
The data suggest that ARCD-1 is a novel cytidine deaminase that interacts with apobec-1 and ACF to inhibit apoB mRNA editing, possibly through interaction with other protein components of the apo B RNA editing holoenzyme. Expand
Cytidine deaminase. The 2.3 A crystal structure of an enzyme: transition-state analog complex.
TLDR
The differences in zinc ligands, ligand-binding stereochemistry, and tertiary structures of CDA and ADA strongly suggest that the common features of transition state stabilization arose by convergent evolution. Expand
An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22.
TLDR
Tissue-specific expression of these genes in a variety of cell lines, along with other evidence, suggests a role for these enzymes in growth or cell cycle control, and similarity in amino acid sequence with APOBEC1, conserved intron/exon organization, tissue- specific expression, homodimerization, and zinc and RNA binding similar to APOB EC1 is concluded. Expand
Crystal structure of the tetrameric cytidine deaminase from Bacillus subtilis at 2.0 A resolution.
TLDR
The first structure of a T-CDA from Bacillus subtilis is determined and reveals that the negative charge caused by the three ligands is partly neutralized by an arginine residue hydrogen-bonded to two of the cysteine residues and the dipoles of two alpha-helices. Expand
The 1.48 A resolution crystal structure of the homotetrameric cytidine deaminase from mouse.
TLDR
Structural analysis further reveals two subclasses of homotetrameric CDAs that can be identified according to the position of the charge-neutralizing arginine residue, suggesting a novel product-expelling mechanism. Expand
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