Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G (Q27649897)

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Elena Harjes

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Phillip J Gross

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Amr Fahmy

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Yongjian Lu

5

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Keisuke Shindo

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Hiroshi Matsuo

APOBEC3G DNA deaminase acts processively 3' --> 5' on single-stranded DNA.

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language of work or name

English

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publication date

6 March 2008

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published in

Nature

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volume

452

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issue

7183

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page(s)

116-9

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cites work

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APOBEC3G cytidine deaminase inhibits retrotransposition of endogenous retroviruses.

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DNA deamination mediates innate immunity to retroviral infection

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Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts

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Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business

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Cytidine deaminase. The 2.3 A crystal structure of an enzyme: transition-state analog complex

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RNA editing enzyme APOBEC1 and some of its homologs can act as DNA mutators

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Crystal structure of the tetrameric cytidine deaminase from Bacillus subtilis at 2.0 A resolution

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Crystal structure of yeast cytosine deaminase. Insights into enzyme mechanism and evolution

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

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The structure of a yeast RNA-editing deaminase provides insight into the fold and function of activation-induced deaminase and APOBEC-1

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Biochemical activities of highly purified, catalytically active human APOBEC3G: correlation with antiviral effect.

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Extensive mutagenesis experiments corroborate a structural model for the DNA deaminase domain of APOBEC3G.

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Complementary function of the two catalytic domains of APOBEC3G.

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Antiviral function of APOBEC3G can be dissociated from cytidine deaminase activity

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Crystal structure of Staphylococcus aureus tRNA adenosine deaminase TadA in complex with RNA.

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Cytidine deamination and resistance to retroviral infection: towards a structural understanding of the APOBEC proteins

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