Evidence map›Paper›PMID 20079749›Full record

ArticleJournal of molecular biology2010

Crystal structure of mouse Elf3 C-terminal DNA-binding domain in complex with type II TGF-beta receptor promoter DNA.

Vinod B Agarkar, Nigar D Babayeva, Phillip J Wilder, Angie Rizzino, Tahir H Tahirov

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

13 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Comparative structure analysis of the ETSi domain of ERG3 and its complex with the E74 promoter DNA sequence.Acta crystallographica. Section F, Structural biology communications · 2018
    Article
  4. Article
  5. Article
  6. Article
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  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Molecular mechanisms of ETS transcription factor-mediated tumorigenesis.Critical reviews in biochemistry and molecular biology
    Review
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

5 authors at 1 institution in 1 country.

Vinod B AgarkarEppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, 987696 Nebraska Medical Center, Omaha, NE 68198-7696, USA.
Nigar D Babayeva
Phillip J Wilder
Angie Rizzino
Tahir H Tahirov
University of Nebraska Medical Center · US

Funding

UNMC/EPPLEY CANCER CENTER SUPPORT GRANTP30CA036727 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI Apar Kishor Ganti · 1985 to 2026
$55.0M
Y-FAMILY POLYMERASES AND CO-FACTORS IN TRANSLESION REPLICATIONP41RR015301 · NCRR · CORNELL UNIVERSITY ITHACA · PI EISENBERG, DAVID · 2001 to 2011
$28.2M
Structural Basis for Synergistic Gene Expression by Runx1 and Ets1 ProteinsR01GM082923 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI TAHIROV, TAHIR H · 2008 to 2012
$1.5M
NCI NIH HHS P30 CA036727NCI NIH HHS P30CA036727NCRR NIH HHS P41 RR015301NCRR NIH HHS RR-15301NIGMS NIH HHS R01 GM082923NIGMS NIH HHS R01GM082923
6 · The paper itself

Abstract

The Ets family of transcription factors is composed of more than 30 members. One of its members, Elf3, is expressed in virtually all epithelial cells as well as in many tumors, including breast tumors. Several studies observed that the promoter of the type II TGF-beta receptor gene (TbetaR-II) is strongly stimulated by Elf3 via two adjacent Elf3 binding sites, the A-site and the B-site. Here, we report the 2.2 A resolution crystal structure of a mouse Elf3 C-terminal fragment, containing the DNA-binding Ets domain, in complex with the B-site of mouse type II TGF-beta receptor promoter DNA (mTbetaR-II(DNA)). Elf3 contacts the core GGAA motif of the B-site from a major groove similar to that of known Ets proteins. However, unlike other Ets proteins, Elf3 also contacts sequences of the A-site from the minor groove of the DNA. DNA binding experiments and cell-based transcription studies indicate that minor groove interaction by Arg349 located in the Ets domain is important for Elf3 function. Equally interesting, previous studies have shown that the C-terminal region of Elf3, which flanks the Ets domain, is required for Elf3 binding to DNA. In this study, we determined that Elf3 amino acid residues within this flanking region, including Trp361, are important for the structural integrity of the protein as well as for the Efl3 DNA binding and transactivation activity.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsBinding SitesCell LineCrystallography, X-RayDNADNA-Binding ProteinsDNA Mutational AnalysisElectrophoretic Mobility Shift AssayHumansMiceMolecular Sequence DataNucleic Acid ConformationPoint MutationPromoter Regions, GeneticDNADNA-Binding ProteinsElf3 protein, mouseProtein Serine-Threonine KinasesProto-Oncogene Proteins c-etsReceptors, Transforming Growth Factor betaReceptor, Transforming Growth Factor-beta Type IITranscription Factors

Identifiers

PMID20079749
PMCPMC2830650
OpenAlexW1998755438

What OpenQuestion holds

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Registered trials

None linked

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.