Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

27 Dec 2014

Abstract excerpt

APOBEC3G (A3G) is a DNA cytidine deaminase (CD) that demonstrates antiviral activity against human immunodeficiency virus 1 (HIV-1) and other pathogenic virus. It has an inactive N-terminal CD1 virus infectivity factor (Vif) protein binding domain (A3G-CD1) and an actively catalytic C-terminal CD2 deamination domain (A3G-CD2). Although many studies on the structure of A3G-CD2 and enzymatic properties of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cytomegalovirus and herpesvirus research
Share to HIV/AIDS drug development and treatment
Share to HIV Research and Treatment

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 25542899
DOI: 10.1074/jbc.m114.624262

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal Structure of DNA Cytidine Deaminase ABOBEC3G Catalytic Deamination Domain Suggests a Binding Mode of Full-length Enzyme to Single-stranded DNAPMID 25542899Read ↗

Crystal Structure of a Soluble APOBEC3G Variant Suggests ssDNA to Bind in a Channel that Extends between the Two Domains.Semantic proximity Read ↗

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

Antiviral Mechanism and Biochemical Basis of the Human APOBEC3 FamilySemantic proximity Read ↗

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

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

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

Structural determinants of human APOBEC3A enzymatic and nucleic acid binding properties.Semantic proximity Read ↗

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

APOBEC3G-Mediated G-to-A Hypermutation of the HIV-1 Genome: The Missing Link in Antiviral Molecular MechanismsSemantic proximity Read ↗

Insights into DNA substrate selection by APOBEC3G from structural, biochemical, and functional studies.Semantic proximity Read ↗

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

Structural Model for Deoxycytidine Deamination Mechanisms of the HIV-1 Inactivation Enzyme APOBEC3GSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.