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 APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificity

28 Apr 2017

Abstract excerpt

Nucleic acid editing enzymes are essential components of the immune system that lethally mutate viral pathogens and somatically mutate immunoglobulins, and contribute to the diversification and lethality of cancers. Among these enzymes are the seven human APOBEC3 deoxycytidine deaminases, each with unique target sequence specificity and subcellular localization. While the enzymology and biological consequences...

Read the complete abstract on PubMed

Topics

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

Share to CRISPR and Genetic Engineering
Share to Cytomegalovirus and herpesvirus research
Share to HIV Research and Treatment

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 28452355
DOI: 10.1038/ncomms15024

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificityPMID 28452355Read ↗

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

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

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

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

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

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

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

Active site plasticity and possible modes of chemical inhibition of the human DNA deaminase APOBEC3BSemantic proximity Read ↗

AID and Apobec3G haphazard deamination and mutational diversity.Semantic proximity Read ↗

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