Evidence map›Paper›PMID 24465866›Full record

ArticlePloS one2014

The molecular basis of conformational instability of the ecdysone receptor DNA binding domain studied by in silico and in vitro experiments.

Agnieszka Szamborska-Gbur, Grzegorz Rymarczyk, Marek Orłowski, Tomasz Kuzynowski, Michał Jakób, Agnieszka Dziedzic-Letka, Andrzej Górecki, Piotr Dobryszycki, Andrzej Ożyhar

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.3field-weighted citation impact, top 50% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

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

9 authors at 2 institutions in 1 country.

Agnieszka Szamborska-GburDepartment of Biochemistry, Faculty of Chemistry, Wrocław University of Technology, Wrocław, Poland.
Grzegorz RymarczykDepartment of Biochemistry, Faculty of Chemistry, Wrocław University of Technology, Wrocław, Poland.
Marek OrłowskiDepartment of Biochemistry, Faculty of Chemistry, Wrocław University of Technology, Wrocław, Poland.
Tomasz KuzynowskiDepartment of Biochemistry, Faculty of Chemistry, Wrocław University of Technology, Wrocław, Poland.
Michał JakóbDepartment of Biochemistry, Faculty of Chemistry, Wrocław University of Technology, Wrocław, Poland.
Agnieszka Dziedzic-LetkaDepartment of Biochemistry, Faculty of Chemistry, Wrocław University of Technology, Wrocław, Poland.
Andrzej GóreckiDepartment of Physical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland.
Piotr DobryszyckiDepartment of Biochemistry, Faculty of Chemistry, Wrocław University of Technology, Wrocław, Poland.
Andrzej OżyharDepartment of Biochemistry, Faculty of Chemistry, Wrocław University of Technology, Wrocław, Poland.
Wrocław University of Science and Technology · PLJagiellonian University · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The heterodimer of the ecdysone receptor (EcR) and ultraspiracle (Usp), members of the nuclear receptors superfamily, regulates gene expression associated with molting and metamorphosis in insects. The DNA binding domains (DBDs) of the Usp and EcR play an important role in their DNA-dependent heterodimerization. Analysis of the crystal structure of the UspDBD/EcRDBD heterocomplex from Drosophila melanogaster on the hsp27 gene response element, suggested an appreciable similarity between both DBDs. However, the chemical denaturation experiments showed a categorically lower stability for the EcRDBD in contrast to the UspDBD. The aim of our study was an elucidation of the molecular basis of this intriguing instability. Toward this end, we mapped the EcRDBD amino acid sequence positions which have an impact on the stability of the EcRDBD. The computational protein design and in vitro analyses of the EcRDBD mutants indicate that non-conserved residues within the α-helix 2, forming the EcRDBD hydrophobic core, represent a specific structural element that contributes to instability. In particular, the L58 appears to be a key residue which differentiates the hydrophobic cores of UspDBD and EcRDBD and is the main reason for the low stability of the EcRDBD. Our results might serve as a benchmark for further studies of the intricate nature of the EcR molecule.

Indexed as

Drosophila melanogasterMolecular Dynamics SimulationAmino Acid SequenceAmino Acid SubstitutionAnimalsBinding SitesDNADNA-Binding ProteinsDrosophila ProteinsHydrophobic and Hydrophilic InteractionsMolecular Sequence DataMutagenesis, Site-DirectedProtein BindingProtein StabilityProtein Structure, SecondaryProtein Structure, TertiaryDNADNA-Binding ProteinsDrosophila Proteinsecdysone receptorReceptors, SteroidTranscription FactorsUSP protein, Drosophila

Identifiers

PMID24465866
PMCPMC3900457
OpenAlexW1993892594

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.