Evidence map›Paper›PMID 38784963›Full record

ArticleCurrent research in structural biology2024

Stability and dynamics of extradenticle modulates its function.

Aakanksha Singh, Bidisha Acharya, Beas Mukherjee, Veda Sheersh Boorla, Soumendu Boral, Snigdha Maiti, Soumya De

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Article in Current research in structural biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. 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

7 authors.

Aakanksha SinghSchool of Bioscience, Indian Institute of Technology Kharagpur, Kharagpur, WB, 721302, India.
Bidisha AcharyaSchool of Bioscience, Indian Institute of Technology Kharagpur, Kharagpur, WB, 721302, India.
Beas MukherjeeSchool of Bioscience, Indian Institute of Technology Kharagpur, Kharagpur, WB, 721302, India.
Veda Sheersh BoorlaSchool of Bioscience, Indian Institute of Technology Kharagpur, Kharagpur, WB, 721302, India.
Soumendu BoralSchool of Bioscience, Indian Institute of Technology Kharagpur, Kharagpur, WB, 721302, India.
Snigdha MaitiSchool of Bioscience, Indian Institute of Technology Kharagpur, Kharagpur, WB, 721302, India.
Soumya DeSchool of Bioscience, Indian Institute of Technology Kharagpur, Kharagpur, WB, 721302, India.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Extradenticle (EXD) is a partner protein of the HOX transcription factors and plays an important role in the development of Drosophila. It confers increased affinity and specificity of DNA-binding to the HOX proteins. However, the DNA-binding homeodomain of EXD has a significantly weaker affinity to DNA compared to the HOX homeodomains. Here, we show that a glycine residue (G290) in the middle of the EXD DNA-binding helix primarily results in this weaker binding. Glycine destabilizes helices. To probe its role in the stability and function of the protein, G290 was mutated to alanine. The intrinsic stability of the DNA-binding helix increased in the G290A mutant as observed by NMR studies and molecular dynamics (MD) simulation. Also, NMR dynamics and MD simulation show that dynamic motions present in the wild-type protein are quenched in the mutant. This in turn resulted in increased stability of the entire homeodomain (ΔΔG

Indexed as

Hydrogen exchangeMD simulationNMR spectroscopyProtein-DNA interactionTranscription factor

Identifiers

PMID38784963
PMCPMC11112286

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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.