Evidence map›Paper›PMID 20159469›Full record

ArticleStructure (London, England : 1993)2010

Crystal structure of the p53 core domain bound to a full consensus site as a self-assembled tetramer.

Yongheng Chen, Raja Dey, Lin Chen

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed, 1 pooled it
5.6field-weighted citation impact, top 3% 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

92 citing papers in PubMed, 1 synthesis or guideline pooled it, 153 citations in OpenAlex.

  1. Targeting p53 pathways: mechanisms, structures, and advances in therapy.Signal transduction and targeted therapy · 2023
    Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. DARPin-induced reactivation of p53 in HPV-positive cells.Nature structural & molecular biology · 2025
    Article
  9. Article
  10. Review
  11. ComparativeProtein and peptide letters · 2025
    Article
  12. Clustering ofiScience · 2024
    Article
  13. Article
  14. Article
  15. Review
  16. A molecular mechanism for the "digital" response of p53 to stress.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  17. Article
  18. Article
  19. Review
  20. Article

32 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Yongheng ChenMolecular and Computational Biology, Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089, USA.
Raja Dey
Lin Chen
University of Southern California · US

Funding

Structural and Functional Versatility of NFATR01GM064642 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI CHEN, LIN · 2005 to 2014
$2.5M
Structure and Function of the FOXP Family of Transcription FactorsR01GM077320 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI CHEN, LIN · 2006 to 2009
$959k
NIGMS NIH HHS R01 GM064642NIGMS NIH HHS R01 GM077320
6 · The paper itself

Abstract

Recent studies suggest that p53 binds predominantly to consensus sites composed of two decameric half-sites with zero spacing in vivo. Here we report the crystal structure of the p53 core domain bound to a full consensus site as a tetramer at 2.13A resolution. Comparison with previously reported structures of p53 dimer:DNA complexes and a chemically trapped p53 tetramer:DNA complex reveals that DNA binding by the p53 core domain is a cooperative self-assembling process accompanied by structural changes of the p53 dimer and DNA. Each p53 monomer interacts with its two neighboring subunits through two different protein-protein interfaces. The DNA is largely B-form and shows no discernible bend, but the central base-pairs between the two half-sites display a significant slide. The extensive protein-protein and protein-DNA interactions explain the high cooperativity and kinetic stability of p53 binding to contiguous decameric sites and the conservation of such binding-site configuration in vivo.

Indexed as

Protein Structure, QuaternaryProtein Structure, TertiaryAmino Acid SequenceAnimalsBinding SitesCrystallography, X-RayDNAHumansMacromolecular SubstancesModels, MolecularMolecular Sequence DataNucleic Acid ConformationProtein BindingProtein MultimerizationSequence AlignmentTumor Suppressor Protein p53DNAMacromolecular SubstancesTumor Suppressor Protein p53

Identifiers

PMID20159469
PMCPMC2824536
OpenAlexW2119742986

What OpenQuestion holds

Textmetadata
LicenceTDM
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.