Evidence map›Paper›PMID 27225672›Full record

ArticleScientific reports2016

Solution structure and binding specificity of the p63 DNA binding domain.

Andreas Enthart, Christian Klein, Alexander Dehner, Murray Coles, Gerd Gemmecker, Horst Kessler, Franz Hagn

Abstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Structural diversity of p63 and p73 isoforms.Cell death and differentiation · 2022
    Review
  6. Article
  7. Review
  8. p63 and p53: Collaborative Partners or Dueling Rivals?Frontiers in cell and developmental biology · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. 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.

Andreas EnthartCenter for Integrated Protein Science Munich (CIPSM) at the Department Chemie, Technische Universität München, 85747 Garching, Germany.
Christian KleinRoche Pharmaceutical Research &Early Development, Roche Innovation Center Zurich, CH-8952 Schlieren, Switzerland.
Alexander DehnerCenter for Integrated Protein Science Munich (CIPSM) at the Department Chemie, Technische Universität München, 85747 Garching, Germany.
Murray ColesDepartment of Protein Evolution, Max-Planck-Institute for Developmental Biology, Tübingen, Germany.
Gerd GemmeckerCenter for Integrated Protein Science Munich (CIPSM) at the Department Chemie, Technische Universität München, 85747 Garching, Germany.
Horst KesslerCenter for Integrated Protein Science Munich (CIPSM) at the Department Chemie, Technische Universität München, 85747 Garching, Germany.
Franz HagnCenter for Integrated Protein Science Munich (CIPSM) at the Department Chemie, Technische Universität München, 85747 Garching, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

p63 is a close homologue of p53 and, together with p73, is grouped into the p53 family of transcription factors. p63 is known to be involved in the induction of controlled apoptosis important for differentiation processes, germ line integrity and development. Despite its high homology to p53, especially within the DNA binding domain (DBD), p63-DBD does not show cooperative DNA binding properties and is significantly more stable against thermal and chemical denaturation. Here, we determined the solution structure of p63-DBD and show that it is markedly less dynamic than p53-DBD. In addition, we also investigate the effect of a double salt bridge present in p53-DBD, but not in p63-DBD on the cooperative binding behavior and specificity to various DNA sites. Restoration of the salt bridges in p63-DBD by mutagenesis leads to enhanced binding affinity to p53-specific, but not p63-specific response elements. Furthermore, we show that p63-DBD is capable of binding to anti-apoptotic BclxL via its DNA binding interface, a feature that has only been shown for p53 so far. These data suggest that all p53 family members - despite alterations in the specificity and binding affinity - are capable of activating pro-apoptotic pathways in a tissue specific manner.

Indexed as

bcl-X ProteinHumansProtein BindingProtein DomainsTranscription FactorsTumor Suppressor ProteinsBCL2L1 protein, humanbcl-X ProteinTP63 protein, humanTranscription FactorsTumor Suppressor Proteins

Identifiers

PMID27225672
PMCPMC4880913

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.