Evidence map›Paper›PMID 35660158›Full record

ArticleStructure (London, England : 1993)2022

A comprehensive structural analysis of the ATPase domain of human DNA topoisomerase II beta bound to AMPPNP, ADP, and the bisdioxopiperazine, ICRF193.

Elise M Ling, Arnaud Baslé, Ian G Cowell, Bert van den Berg, Tim R Blower, Caroline A Austin

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

17 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Structural Mechanisms of Topoisomerase-Targeting Drugs.Annual review of biochemistry · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Recombinant Topoisomerase 2 Production Using Cultured Human Cell Lines.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. 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

6 authors at 2 institutions in 1 country.

Elise M LingBiosciences Institute, Newcastle University, Newcastle upon Tyne NE2 4HH, UK.
Arnaud BasléBiosciences Institute, Newcastle University, Newcastle upon Tyne NE2 4HH, UK.
Ian G CowellBiosciences Institute, Newcastle University, Newcastle upon Tyne NE2 4HH, UK.
Bert van den BergBiosciences Institute, Newcastle University, Newcastle upon Tyne NE2 4HH, UK.
Tim R BlowerDepartment of Biosciences, Durham University, South Road, Durham DH1 3LE, UK. Electronic address: timothy.blower@durham.ac.uk.
Caroline A AustinBiosciences Institute, Newcastle University, Newcastle upon Tyne NE2 4HH, UK. Electronic address: caroline.austin@ncl.ac.uk.
Newcastle University · GBDurham University · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M011186/1
6 · The paper itself

Abstract

Human topoisomerase II beta (TOP2B) modulates DNA topology using energy from ATP hydrolysis. To investigate the conformational changes that occur during ATP hydrolysis, we determined the X-ray crystallographic structures of the human TOP2B ATPase domain bound to AMPPNP or ADP at 1.9 Å and 2.6 Å resolution, respectively. The GHKL domains of both structures are similar, whereas the QTK loop within the transducer domain can move for product release. As TOP2B is the clinical target of bisdioxopiperazines, we also determined the structure of a TOP2B:ADP:ICRF193 complex to 2.3 Å resolution and identified key drug-binding residues. Biochemical characterization revealed the N-terminal strap reduces the rate of ATP hydrolysis. Mutagenesis demonstrated residue E103 as essential for ATP hydrolysis in TOP2B. Our data provide fundamental insights into the tertiary structure of the human TOP2B ATPase domain and a potential regulatory mechanism for ATP hydrolysis.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateDNA Topoisomerases, Type IIAdenosine DiphosphateAdenylyl ImidodiphosphateHumansHydrolysisPoly-ADP-Ribose Binding ProteinsAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateAdenylyl ImidodiphosphateDNA Topoisomerases, Type IIPoly-ADP-Ribose Binding ProteinsTOP2B protein, humanATPase activityATPase domain structureBergerat foldbiochemistrybisdioxopiperazinecrystallographyGHKL-type ATPaseICRF193N-terminal strapTOP2B

Identifiers

PMID35660158
PMCPMC9592559
OpenAlexW4281781140

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.