Evidence map›Paper›PMID 28452355›Full record

ArticleNature communications2017

Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificity.

Takahide Kouno, Tania V Silvas, Brendan J Hilbert, Shivender M D Shandilya, Markus F Bohn, Brian A Kelch, William E Royer, Mohan Somasundaran, Nese Kurt Yilmaz, Hiroshi Matsuo and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers.

0numbers the graph read from it
0cells of the map it votes in
116citing papers in PubMed
9.0field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

116 citing papers in PubMed, 162 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Two codes of RNA editing by deamination in human diseases.Experimental & molecular medicine · 2026
    Review
  7. HAMMER: Hairpin-based APOBEC3A-mediated mRNA editing reporter.bioRxiv : the preprint server for biology · 2026
    Article
  8. Review
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56 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 2 institutions in 1 country.

Takahide KounoDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01655, USA.
Tania V SilvasDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01655, USA.
Brendan J HilbertDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01655, USA.
Shivender M D ShandilyaDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01655, USA.
Markus F BohnDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01655, USA.
Brian A KelchDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01655, USA.
William E RoyerDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01655, USA.
Mohan SomasundaranProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts 01655, USA.
Nese Kurt YilmazDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01655, USA.
Hiroshi MatsuoBasic Research Laboratory, Leidos Biomedical Research, Inc., Frederick National Laboratory, Frederick, Maryland 21702, USA.
Celia A SchifferDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01655, USA.
University of Massachusetts Chan Medical School · USLeidos (United States) · US

Funding

Structural Characterization of APOBECS's Atomic interactionsP01GM091743 · NIGMS · UNIVERSITY OF MINNESOTA · PI MATSUO, HIROSHI · 2011 to 2015
$10.1M
Structural studies of biomolecules related to cancer and HIV-AIDSZICBC011849 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI MATSUO, HIROSHI · 2018 to 2024
$5.0M
Structurally dissecting APOBEC3's for HIV-1 restrictionR01GM118474 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI SCHIFFER, CELIA A. · 2016 to 2018
$1.8M
Structural studies of biomolecules related to cancer and HIV-AIDSZIABC011717 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI MATSUO, HIROSHI · 2016 to 2017
$1.4M
Macromolecular Crystallographic HighFlux Home Lab X-ray Diffraction SystemS10OD012028 · OD · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI SCHIFFER, CELIA A. · 2012 to 2012
$531k
Structural basis for substrate specificity of single domain APOBEC3sF31GM119931 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI SILVAS, TANIA VANESSA · 2016 to 2017
$59k
NIGMS NIH HHS F31 GM119931NIGMS NIH HHS P01 GM091743NIGMS NIH HHS R01 GM118474NIH HHS S10 OD012028
6 · The paper itself

Abstract

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 have been extensively studied, the mechanism by which APOBEC3s recognize and edit DNA remains elusive. Here we present the crystal structure of a complex of a cytidine deaminase with ssDNA bound in the active site at 2.2 Å. This structure not only visualizes the active site poised for catalysis of APOBEC3A, but pinpoints the residues that confer specificity towards CC/TC motifs. The APOBEC3A-ssDNA complex defines the 5'-3' directionality and subtle conformational changes that clench the ssDNA within the binding groove, revealing the architecture and mechanism of ssDNA recognition that is likely conserved among all polynucleotide deaminases, thereby opening the door for the design of mechanistic-based therapeutics.

Indexed as

Catalytic DomainAmino Acid SequenceCrystallography, X-RayCytidineCytidine DeaminaseDeaminationDNA, Single-StrandedHumansModels, MolecularProtein BindingProtein DomainsProteinsProtein Structure, SecondarySequence Homology, Amino AcidSubstrate SpecificityAPOBEC3A protein, humanCytidineCytidine DeaminaseDNA, Single-StrandedProteins

Identifiers

PMID28452355
PMCPMC5414352
OpenAlexW2608375766

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.