Evidence map›Paper›PMID 31723028›Full record

ArticleThe Journal of biological chemistry2019

Structural basis of binding of homodimers of the nuclear receptor NR4A2 to selective Nur-responsive DNA elements.

Longying Jiang, Shuyan Dai, Jun Li, Xujun Liang, Lingzhi Qu, Xiaojuan Chen, Ming Guo, Zhuchu Chen, Lin Chen, Hudie Wei and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed, 1 pooled it
2.1field-weighted citation impact, top 14% 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, 1 synthesis or guideline pooled it, 29 citations in OpenAlex.

  1. PROKR1-CREB-NR4A2 axis for oxidative muscle fiber specification and improvement of metabolic function.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Pooled it
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Integrative analysis reveals structural basis for transcription activation of Nurr1 and Nurr1-RXRα heterodimer.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Article
  9. Article
  10. Nurr1 Modulation Mediates Neuroprotective Effects of Statins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. 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

11 authors at 2 institutions in 2 countries.

Longying JiangDepartment of Oncology, Laboratory of Structural Biology, NHC Key Laboratory of Cancer Proteomics, Xiangya Hospital, Central South University, Changsha, Hunan 410008, China.
Shuyan DaiDepartment of Oncology, Laboratory of Structural Biology, NHC Key Laboratory of Cancer Proteomics, Xiangya Hospital, Central South University, Changsha, Hunan 410008, China.ORCID 0000-0002-8484-634X
Jun LiDepartment of Oncology, Laboratory of Structural Biology, NHC Key Laboratory of Cancer Proteomics, Xiangya Hospital, Central South University, Changsha, Hunan 410008, China.
Xujun LiangDepartment of Oncology, Laboratory of Structural Biology, NHC Key Laboratory of Cancer Proteomics, Xiangya Hospital, Central South University, Changsha, Hunan 410008, China.
Lingzhi QuDepartment of Oncology, Laboratory of Structural Biology, NHC Key Laboratory of Cancer Proteomics, Xiangya Hospital, Central South University, Changsha, Hunan 410008, China.
Xiaojuan ChenDepartment of Oncology, Laboratory of Structural Biology, NHC Key Laboratory of Cancer Proteomics, Xiangya Hospital, Central South University, Changsha, Hunan 410008, China.
Ming GuoDepartment of Oncology, Laboratory of Structural Biology, NHC Key Laboratory of Cancer Proteomics, Xiangya Hospital, Central South University, Changsha, Hunan 410008, China.
Zhuchu ChenDepartment of Oncology, Laboratory of Structural Biology, NHC Key Laboratory of Cancer Proteomics, Xiangya Hospital, Central South University, Changsha, Hunan 410008, China.
Lin ChenDepartment of Oncology, Laboratory of Structural Biology, NHC Key Laboratory of Cancer Proteomics, Xiangya Hospital, Central South University, Changsha, Hunan 410008, China.
Hudie WeiDepartment of Oncology, Laboratory of Structural Biology, NHC Key Laboratory of Cancer Proteomics, Xiangya Hospital, Central South University, Changsha, Hunan 410008, China hudiewei18@163.com.
Yongheng ChenDepartment of Oncology, Laboratory of Structural Biology, NHC Key Laboratory of Cancer Proteomics, Xiangya Hospital, Central South University, Changsha, Hunan 410008, China yonghenc@163.com.
Central South University · CNUniversity of Southern California · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins of nuclear receptor subfamily 4 group A (NR4A), including NR4A1/NGFI-B, NR4A2/Nurr1, and NR4A3/NOR-1, are nuclear transcription factors that play important roles in metabolism, apoptosis, and proliferation. NR4A proteins recognize DNA response elements as monomers or dimers to regulate the transcription of a variety of genes involved in multiple biological processes. In this study, we determined two crystal structures of the NR4A2 DNA-binding domain (NR4A2-DBD) bound to two Nur-responsive elements: an inverted repeat and an everted repeat at 2.6-2.8 Å resolution. The structures revealed that two NR4A2-DBD molecules bind independently to the everted repeat, whereas two other NR4A2-DBD molecules form a novel dimer interface on the inverted repeat. Moreover, substitution of the interfacial residue valine 298 to lysine as well as mutation of DNA bases involved in the interactions abolished the dimerization. Overall, our structural, biochemical, and bioinformatics analyses provide a molecular basis for the binding of the NR4A2 protein dimers to NurREs and advance our understanding of the dimerization specificity of nuclear receptors.

Indexed as

Amino Acid MotifsApoptosisCell NucleusCell ProliferationDimerizationDNAEscherichia coliHumansLysineMutationNuclear Receptor Subfamily 4, Group A, Member 2Protein BindingProtein Interaction MappingRetinoid X ReceptorsTranscription, GeneticValineDNALysineNR4A2 protein, humanNuclear Receptor Subfamily 4, Group A, Member 2Retinoid X ReceptorsValinecrystal structuredimerizationgene regulationnuclear receptornuclear receptor subfamily 4 group A member 2Nur-responsive elementsprotein crystallizationprotein–DNA interactionprotein–protein interactiontranscription factor

Identifiers

PMID31723028
PMCPMC6926456
OpenAlexW2983833212

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.