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 the catalytic domain of HIV-1 restriction factor APOBEC3G in complex with ssDNA

19 Jun 2018

Abstract excerpt

The human APOBEC3G protein is a cytidine deaminase that generates cytidine to deoxy-uridine mutations in single-stranded DNA (ssDNA), and capable of restricting replication of HIV-1 by generating mutations in viral genome. The mechanism by which APOBEC3G specifically deaminates 5'-CC motifs has remained elusive since structural studies have been hampered due to apparently weak ssDNA binding of the catalytic...

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: 29941968
DOI: 10.1038/s41467-018-04872-8

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal structure of the catalytic domain of HIV-1 restriction factor APOBEC3G in complex with ssDNAPMID 29941968Read ↗

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

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

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

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

Substrate sequence selectivity of APOBEC3A implicates intra-DNA interactionsSemantic proximity Read ↗

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

Substrate sequence selectivity of APOBEC3A implicates intra-DNA interactions.Semantic proximity Read ↗

Loop 1 of APOBEC3C regulates its antiviral activity against HIV-1Semantic proximity Read ↗

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

The ssDNA Mutator APOBEC3A Is Regulated by Cooperative Dimerization.Semantic proximity Read ↗

Structural perspectives on HIV‐1 Vif and APOBEC3 restriction factor interactionsSemantic proximity Read ↗

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