Evidence map›Paper›PMID 31162607›Full record

ArticleNucleic acids research2019

The HRP3 PWWP domain recognizes the minor groove of double-stranded DNA and recruits HRP3 to chromatin.

Wei Tian, Peiqiang Yan, Ning Xu, Arghya Chakravorty, Robert Liefke, Qiaoran Xi, Zhanxin Wang

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 32 citations in OpenAlex.

  1. NMR Studies on Protein-Ligand Interactions.International journal of molecular sciences · 2026
    Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Binding Behavior of Human Hepatoma-Derived Growth Factor onThe journal of physical chemistry. B · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. 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 at 4 institutions in 3 countries.

Wei TianKey Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University, 19 Xinjiekouwai Avenue, Beijing 100875, China.
Peiqiang YanMOE Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Ning XuBeijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Arghya ChakravortyDepartment of Physics and Astronomy, Clemson University, Clemson, SC 29634, USA.
Robert LiefkeInstitute of Molecular Biology and Tumor Research (IMT), Philipps University of Marburg, Marburg 35043, Germany.
Qiaoran XiMOE Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Zhanxin WangKey Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University, 19 Xinjiekouwai Avenue, Beijing 100875, China.
Tsinghua University · CNBeijing Normal University · CNClemson University · USPhilipps University of Marburg · DE

Funding

New Generation DelPhi: large systems and beyond electrostaticsR01GM093937 · NIGMS · CLEMSON UNIVERSITY · PI ALEXOV, EMIL GEORGIEV · 2010 to 2023
$4.3M
NIGMS NIH HHS R01 GM093937
6 · The paper itself

Abstract

HDGF-related protein 3 (HRP3, also known as HDGFL3) belongs to the family of HDGF-related proteins (HRPs) and plays an essential role in hepatocellular carcinoma pathogenesis. All HRPs have a PWWP domain at the N-terminus that binds both histone and DNA substrates. Despite previous advances in PWWP domains, the molecular basis by which HRP3 interacts with chromatin is unclear. In this study, we solved the crystal structures of the HRP3 PWWP domain in complex with various double-stranded DNAs with/without bound histone peptides. We found that HRP3 PWWP bound to the phosphate backbone of the DNA minor groove and showed a preference for DNA molecules bearing a narrow minor groove width. In addition, HRP3 PWWP preferentially bound to histone peptides bearing the H3K36me3/2 modification. HRP3 PWWP uses two adjacent surfaces to bind both DNA and histone substrates simultaneously, enabling us to generate a model illustrating the recruitment of PWWP to H3K36me3-containing nucleosomes. Cell-based analysis indicated that both DNA and histone binding by the HRP3 PWWP domain is important for HRP3 recruitment to chromatin in vivo. Our work establishes that HRP3 PWWP is a new family of minor groove-specific DNA-binding proteins, which improves our understanding of HRP3 and other PWWP domain-containing proteins.

Indexed as

AnimalsBinding SitesChromatinCrystallography, X-RayCytoskeletal ProteinsDNAHEK293 CellsHep G2 CellsHistonesHumansIntracellular Signaling Peptides and ProteinsMagnetic Resonance SpectroscopyNuclear ProteinsNucleic Acid ConformationNucleosomesPeptidesChromatinCytoskeletal ProteinsDNAHDGFL3 protein, humanHistonesIntracellular Signaling Peptides and ProteinsNuclear ProteinsNucleosomesPeptides

Identifiers

PMID31162607
PMCPMC6547440
OpenAlexW2941950483

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.