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Article

Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications.

Nature - 6 Nov 2008

Holden Lauren G, Prochnow Courtney, Chang Y Paul, Bransteitter Ronda, Chelico Linda, Sen Udayaditya, Stevens Raymond C, Goodman Myron F, Chen Xiaojiang S

Abstract excerpt

The APOBEC family members are involved in diverse biological functions. APOBEC3G restricts the replication of human immunodeficiency virus (HIV), hepatitis B virus and retroelements by cytidine deamination on single-stranded DNA or by RNA binding. Here we report the high-resolution crystal structure of the carboxy-terminal deaminase domain of APOBEC3G (APOBEC3G-CD2) purified from Escherichia coli. The...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 18849968
DOI: 10.1038/nature07357
PMCID: PMC2714533

Genes

APOBEC2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications.PMID 18849968Read ↗

Structural basis of substrate specificity in human cytidine deaminase family APOBEC3s.Semantic proximity Read ↗

Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificitySemantic proximity Read ↗

Crystal Structure of DNA Cytidine Deaminase ABOBEC3G Catalytic Deamination Domain Suggests a Binding Mode of Full-length Enzyme to Single-stranded DNASemantic proximity Read ↗

Crystal structure of the catalytic domain of HIV-1 restriction factor APOBEC3G in complex with ssDNASemantic proximity Read ↗

Structural analysis of the active site and DNA binding of human cytidine deaminase APOBEC3BSemantic proximity Read ↗

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Role of the single deaminase domain APOBEC3A in virus restriction, retrotransposition, DNA damage and cancerSemantic proximity Read ↗

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