Evidence map›Paper›PMID 28652322›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Cryo-EM structure of the DNA-PK holoenzyme.

Humayun Sharif, Yang Li, Yuanchen Dong, Liyi Dong, Wei Li Wang, Youdong Mao, Hao Wu

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

51 citing papers in PubMed, 80 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Review
  5. Review
  6. Identification of 6-Anilino Imidazo[4,5-Journal of medicinal chemistry · 2024
    Article
  7. Secrets of DNA-PKcs beyond DNA repair.NPJ precision oncology · 2024
    Review
  8. Review
  9. Article
  10. A Phase Ib Study of the DNA-PK Inhibitor Peposertib Combined with Neoadjuvant Chemoradiation in Patients with Locally Advanced Rectal Cancer.Clinical cancer research : an official journal of the American Association for Cancer Research · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Human DNA-dependent protein kinase activation mechanism.Nature structural & molecular biology · 2023
    Article
  18. Review
  19. Article
  20. 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 2 countries.

Humayun SharifDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.
Yang LiDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.
Yuanchen DongDepartment of Cancer Immunology and Virology, Intel Parallel Computing Center for Structural Biology, Dana-Farber Cancer Institute, Boston, MA 02215.
Liyi DongDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.
Wei Li WangDepartment of Cancer Immunology and Virology, Intel Parallel Computing Center for Structural Biology, Dana-Farber Cancer Institute, Boston, MA 02215.
Youdong MaoDepartment of Cancer Immunology and Virology, Intel Parallel Computing Center for Structural Biology, Dana-Farber Cancer Institute, Boston, MA 02215.
Hao WuDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115; wu@crystal.harvard.edu.
Boston Children's Hospital · USIntel (United States) · USDana-Farber Cancer Institute · USHarvard University · US

Funding

Virus biology scientific research support componentUM1AI100645 · NIAID · DUKE UNIVERSITY · PI KEPLER, THOMAS B · 2012 to 2018
$204.7M
Molecular mechanisms of the RAG recombinase in V(D)J recombination and diseaseR01AI125535 · NIAID · BOSTON CHILDREN'S HOSPITAL · PI WU, HAO · 2016 to 2020
$3.2M
NIAID NIH HHS R01 AI125535NIAID NIH HHS UM1 AI100645
6 · The paper itself

Abstract

DNA-dependent protein kinase (DNA-PK) is a large protein complex central to the nonhomologous end joining (NHEJ) DNA-repair pathway. It comprises the DNA-PK catalytic subunit (DNA-PKcs) and the heterodimer of DNA-binding proteins Ku70 and Ku80. Here, we report the cryo-electron microscopy (cryo-EM) structures of human DNA-PKcs at 4.4-Å resolution and the DNA-PK holoenzyme at 5.8-Å resolution. The DNA-PKcs structure contains three distinct segments: the N-terminal region with an arm and a bridge, the circular cradle, and the head that includes the kinase domain. Two perpendicular apertures exist in the structure, which are sufficiently large for the passage of dsDNA. The DNA-PK holoenzyme cryo-EM map reveals density for the C-terminal globular domain of Ku80 that interacts with the arm of DNA-PKcs. The Ku80-binding site is adjacent to the previously identified density for the DNA-binding region of the Ku70/Ku80 complex, suggesting concerted DNA interaction by DNA-PKcs and the Ku complex.

Indexed as

Cryoelectron MicroscopyCatalysisCatalytic DomainCrystallography, X-RayDNA-Activated Protein KinaseDNA Breaks, Double-StrandedDNA RepairHeLa CellsHumansKu AutoantigenNuclear ProteinsProtein BindingDNA-Activated Protein KinaseKu AutoantigenNuclear ProteinsPRKDC protein, humancryo-EMDNA repairNHEJstructureV(D)J recombination

Identifiers

PMID28652322
PMCPMC5514765
OpenAlexW2660877075

What OpenQuestion holds

Textmetadata
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.