Evidence map›Paper›PMID 24682817›Full record

ArticleNucleic acids research2014

Distinct Z-DNA binding mode of a PKR-like protein kinase containing a Z-DNA binding domain (PKZ).

Doyoun Kim, Jeonghwan Hur, Kwangsoo Park, Sangsu Bae, Donghyuk Shin, Sung Chul Ha, Hye-Yeon Hwang, Sungchul Hohng, Joon-Hwa Lee, Sangho Lee and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.9field-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

31 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
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  7. Review
  8. Article
  9. Z-DNA and Z-RNA: Methods-Past and Future.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Characterization of Z-DNA Using Circular Dichroism.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Dynamics Studies of DNA with Non-canonical Structure Using NMR Spectroscopy.International journal of molecular sciences · 2020
    Review
  18. Review
  19. Review
  20. 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

12 authors at 5 institutions in 1 country.

Doyoun KimDepartment of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea.
Jeonghwan HurDepartment of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea.
Kwangsoo ParkDepartment of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea.
Sangsu BaeDepartment of Physics and Astronomy, Seoul National University, Seoul 151-747, Korea National Center for Creative Research Initiatives, Seoul National University, Seoul 151-747, Korea.
Donghyuk ShinDepartment of Biological Sciences, Sungkyunkwan University, Suwon 440-746, Korea.
Sung Chul HaPohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang, Kyungbuk 790-784, Korea.
Hye-Yeon HwangDepartment of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea.
Sungchul HohngDepartment of Physics and Astronomy, Seoul National University, Seoul 151-747, Korea National Center for Creative Research Initiatives, Seoul National University, Seoul 151-747, Korea Department of Biophysics and Chemical Biology, Seoul National University, Seoul 151-747, Korea.
Joon-Hwa LeeDepartment of Chemistry and RINS, Gyeongsang National University, Jinju, Gyeongnam 660-701, Korea.
Sangho LeeDepartment of Biological Sciences, Sungkyunkwan University, Suwon 440-746, Korea.
Yang-Gyun KimDepartment of Chemistry, Sungkyunkwan University, Suwon 440-746, Korea kyeongkyu@skku.edu.
Kyeong Kyu KimDepartment of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea kyeongkyu@skku.edu.
Sungkyunkwan University · KRSeoul National University · KRGyeongsang National University · KRPohang University of Science and Technology · KRSamsung (South Korea) · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Double-stranded ribonucleic acid-activated protein kinase (PKR) downregulates translation as a defense mechanism against viral infection. In fish species, PKZ, a PKR-like protein kinase containing left-handed deoxyribonucleic acid (Z-DNA) binding domains, performs a similar role in the antiviral response. To understand the role of PKZ in Z-DNA recognition and innate immune response, we performed structural and functional studies of the Z-DNA binding domain (Zα) of PKZ from Carassius auratus (caZαPKZ). The 1.7-Å resolution crystal structure of caZαPKZ:Z-DNA revealed that caZαPKZ shares the overall fold with other Zα, but has discrete structural features that differentiate its DNA binding mode from others. Functional analyses of caZαPKZ and its mutants revealed that caZαPKZ mediates the fastest B-to-Z transition of DNA among Zα, and the minimal interaction for Z-DNA recognition is mediated by three backbone phosphates and six residues of caZαPKZ. Structure-based mutagenesis and B-to-Z transition assays confirmed that Lys56 located in the β-wing contributes to its fast B-to-Z transition kinetics. Investigation of the DNA binding kinetics of caZαPKZ further revealed that the B-to-Z transition rate is positively correlated with the association rate constant. Taking these results together, we conclude that the positive charge in the β-wing largely affects fast B-to-Z transition activity by enhancing the DNA binding rate.

Indexed as

GoldfishAmino Acid SequenceAnimalsCatalytic DomainCrystallography, X-RayDNA, Z-FormeIF-2 KinaseFish ProteinsHydrogen BondingKineticsModels, MolecularMolecular Sequence DataProtein Structure, SecondarySodium ChlorideDNA, Z-FormeIF-2 KinaseFish ProteinsSodium Chloride

Identifiers

PMID24682817
PMCPMC4027156
OpenAlexW2106474338

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.