Evidence map›Paper›PMID 38130056›Full record

ArticleBiophysical journal2024

Probing the role of the protonation state of a minor groove-linker histidine in Exd-Hox-DNA binding.

Yibei Jiang, Tsu-Pei Chiu, Raktim Mitra, Remo Rohs

Open access · hybridAbstract read
In one paragraph

Article in Biophysical journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

7 citing papers in PubMed, 8 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

Yibei JiangDepartment of Quantitative and Computational Biology, University of Southern California, Los Angeles, California.
Tsu-Pei ChiuDepartment of Quantitative and Computational Biology, University of Southern California, Los Angeles, California.
Raktim MitraDepartment of Quantitative and Computational Biology, University of Southern California, Los Angeles, California.
Remo RohsDepartment of Quantitative and Computational Biology, University of Southern California, Los Angeles, California; Department of Chemistry, University of Southern California, Los Angeles, California; Department of Physics and Astronomy, University of Southern California, Los Angeles, California; Thomas Lord Department of Computer Science, University of Southern California, Los Angeles, California. Electronic address: rohs@usc.edu.
University of Southern California · US

Funding

Quantitative Modeling of Transcription Factor-DNA BindingR35GM130376 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI Remo Rohs · 2019 to 2026
$3.3M
NIGMS NIH HHS R35 GM130376
6 · The paper itself

Abstract

DNA recognition and targeting by transcription factors (TFs) through specific binding are fundamental in biological processes. Furthermore, the histidine protonation state at the TF-DNA binding interface can significantly influence the binding mechanism of TF-DNA complexes. Nevertheless, the role of histidine in TF-DNA complexes remains underexplored. Here, we employed all-atom molecular dynamics simulations using AlphaFold2-modeled complexes based on previously solved co-crystal structures to probe the role of the His-12 residue in the Extradenticle (Exd)-Sex combs reduced (Scr)-DNA complex when binding to Scr and Ultrabithorax (Ubx) target sites. Our results demonstrate that the protonation state of histidine notably affected the DNA minor-groove width profile and binding free energy. Examining flanking sequences of various binding affinities derived from SELEX-seq experiments, we analyzed the relationship between binding affinity and specificity. We uncovered how histidine protonation leads to increased binding affinity but can lower specificity. Our findings provide new mechanistic insights into the role of histidine in modulating TF-DNA binding.

Indexed as

Drosophila ProteinsHomeodomain ProteinsAnimalsBinding SitesDNADrosophila melanogasterHistidineTranscription FactorsDNADrosophila ProteinsHistidineHomeodomain ProteinsTranscription FactorsUbx protein, Drosophila

Identifiers

PMID38130056
PMCPMC10808038
OpenAlexW4390024730

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.