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Article

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

FEBS letters - 2 Oct 2007

Chen Kuan-Ming, Martemyanova Natalia, Lu Yongjian, Shindo Keisuke, Matsuo Hiroshi, Harris Reuben S

Abstract excerpt

APOBEC3G is a single-strand DNA cytosine deaminase capable of blocking retrovirus and retrotransposon replication. APOBEC3G has two conserved zinc-coordinating motifs but only one is required for catalysis. Here, deletion analyses revealed that the minimal catalytic domain consists of residues 198-384. Size exclusion assays indicated that this protein is monomeric. Many (31/69) alanine substitution derivatives of...

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Topics

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Share to Amino Acid Motifs
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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Share to Cytidine Deaminase

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Source

Open in PubMed Open full text

Identifiers

PMID: 17869248
DOI: 10.1016/j.febslet.2007.08.076
PMCID: PMC2014798

Genes

APOBEC2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

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Extensive mutagenesis experiments corroborate a structural model for the DNA deaminase domain of APOBEC3G.PMID 17869248Read ↗

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