Evidence map›Paper›PMID 25984970›Full record

ArticleNature structural & molecular biology2015

Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G.

Takahide Kouno, Elizabeth M Luengas, Megumi Shigematsu, Shivender M D Shandilya, JingYing Zhang, Luan Chen, Mayuko Hara, Celia A Schiffer, Reuben S Harris, Hiroshi Matsuo

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed, 1 pooled it
6.3field-weighted citation impact, top 3% 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

60 citing papers in PubMed, 1 synthesis or guideline pooled it, 79 citations in OpenAlex.

  1. HIV Genome-Wide Protein Associations: a Review of 30 Years of Research.Microbiology and molecular biology reviews : MMBR · 2016
    Pooled it
  2. Review
  3. Article
  4. Article
  5. Article
  6. HIV-1 Vif protein sequence variations in South African people living with HIV and their influence on Vif-APOBEC3G interaction.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2024
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. The current toolbox for APOBEC drug discovery.Trends in pharmacological sciences · 2022
    Review
  15. Article
  16. Interactions of APOBEC3s with DNA and RNA.Current opinion in structural biology · 2021
    Review
  17. Review
  18. Characterization of an A3G-VifMolecular & cellular proteomics : MCP · 2021
    Article
  19. Review
  20. Article
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

10 authors at 1 institution in 1 country.

Takahide Kouno1] Biochemistry, Molecular Biology and Biophysics Department, Institute for Molecular Virology, University of Minnesota, Minneapolis, Minnesota, USA. [2] Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts, USA.
Elizabeth M LuengasBiochemistry, Molecular Biology and Biophysics Department, Masonic Cancer Center, Center for Genome Engineering, Institute for Molecular Virology, University of Minnesota, Minneapolis, Minnesota, USA.
Megumi ShigematsuBiochemistry, Molecular Biology and Biophysics Department, Institute for Molecular Virology, University of Minnesota, Minneapolis, Minnesota, USA.
Shivender M D ShandilyaDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts, USA.
JingYing ZhangBiochemistry, Molecular Biology and Biophysics Department, Institute for Molecular Virology, University of Minnesota, Minneapolis, Minnesota, USA.
Luan ChenBiochemistry, Molecular Biology and Biophysics Department, Institute for Molecular Virology, University of Minnesota, Minneapolis, Minnesota, USA.
Mayuko HaraBiochemistry, Molecular Biology and Biophysics Department, Institute for Molecular Virology, University of Minnesota, Minneapolis, Minnesota, USA.
Celia A SchifferDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts, USA.
Reuben S HarrisBiochemistry, Molecular Biology and Biophysics Department, Masonic Cancer Center, Center for Genome Engineering, Institute for Molecular Virology, University of Minnesota, Minneapolis, Minnesota, USA.
Hiroshi MatsuoBiochemistry, Molecular Biology and Biophysics Department, Institute for Molecular Virology, University of Minnesota, Minneapolis, Minnesota, USA.
University of Massachusetts Chan Medical School · US

Funding

Structural Characterization of APOBECS's Atomic interactionsP01GM091743 · NIGMS · UNIVERSITY OF MINNESOTA · PI KOTLER, MOSHE · 2011 to 2015
$10.1M
Structural Studies of Human APOBEC3G and HIV VifR33AI073167 · NIAID · UNIVERSITY OF MINNESOTA · PI MATSUO, HIROSHI · 2009 to 2011
$1.2M
Structural Studies of Human APOBEC3G and HIV VifR21AI073167 · NIAID · UNIVERSITY OF MINNESOTA · PI MATSUO, HIROSHI · 2007 to 2008
$397k
NIAID NIH HHS AI073167NIAID NIH HHS R21 AI073167NIAID NIH HHS R33 AI073167NIGMS NIH HHS GM091743NIGMS NIH HHS P01 GM091743
6 · The paper itself

Abstract

The human APOBEC3G (A3G) DNA cytosine deaminase restricts and hypermutates DNA-based parasites including HIV-1. The viral infectivity factor (Vif) prevents restriction by triggering A3G degradation. Although the structure of the A3G catalytic domain is known, the structure of the N-terminal Vif-binding domain has proven more elusive. Here, we used evolution- and structure-guided mutagenesis to solubilize the Vif-binding domain of A3G, thus permitting structural determination by NMR spectroscopy. A smaller zinc-coordinating pocket and altered helical packing distinguish the structure from previous catalytic-domain structures and help to explain the reported inactivity of this domain. This soluble A3G N-terminal domain is bound by Vif; this enabled mutagenesis and biochemical experiments, which identified a unique Vif-interacting surface formed by the α1-β1, β2-α2 and β4-α4 loops. This structure sheds new light on the Vif-A3G interaction and provides critical information for future drug development.

Indexed as

APOBEC-3G DeaminaseCytidine DeaminaseDNA Mutational AnalysisHumansMagnetic Resonance SpectroscopyModels, MolecularMutant ProteinsProtein BindingProtein ConformationProtein Interaction Mappingvif Gene Products, Human Immunodeficiency VirusAPOBEC-3G DeaminaseAPOBEC3G protein, humanCytidine DeaminaseMutant Proteinsvif Gene Products, Human Immunodeficiency Virusvif protein, Human immunodeficiency virus 1

Identifiers

PMID25984970
PMCPMC4456288
OpenAlexW1881970551

What OpenQuestion holds

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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.