Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain.

Proceedings of the National Academy of Sciences of the United States of America - 15 Apr 2008

Wells Mark, Tidow Henning, Rutherford Trevor J, Markwick Phineus, Jensen Malene Ringkjobing, Mylonas Efstratios, Svergun Dmitri I, Blackledge Martin, Fersht Alan R

Abstract excerpt

Proteins with intrinsically disordered domains are implicated in a vast range of biological processes, especially in cell signaling and regulation. Having solved the quaternary structure of the folded domains in the tumor suppressor p53 by a multidisciplinary approach, we have now determined the average ensemble structure of the intrinsically disordered N-terminal transactivation domain (TAD) by using residual...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Peptide Fragments
Share to Amino Acid Motifs

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Protein Structure, Tertiary

Share to Response Elements

Share to Scattering, Small Angle

Share to Transcriptional Activation

Share to Tumor Suppressor Protein p53

Share to X-Ray Diffraction

Source

Open in PubMed Open full text

Identifiers

PMID: 18391200
DOI: 10.1073/pnas.0801353105
PMCID: PMC2311362

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain.PMID 18391200Read ↗

Cancer-Associated Mutations Perturb the Structure and Interactions of the Intrinsically Disordered p53 Transactivation DomainSemantic proximity Read ↗

Cancer-Associated Mutations Perturb the Disordered Ensemble and Interactions of the Intrinsically Disordered p53 Transactivation Domain.Semantic proximity Read ↗

Structural Assessment of the Full-Length Wild-Type Tumor Suppressor Protein p53 by Mass Spectrometry-Guided Computational ModelingSemantic proximity Read ↗

Structural Assessment of the Full-Length Wild-Type Tumor Suppressor Protein p53 by Mass Spectrometry-Guided Computational ModelingSemantic proximity Read ↗

Modulation of the disordered conformational ensembles of the p53 transactivation domain by cancer-associated mutations.Semantic proximity Read ↗

Modulation of p53 Transactivation Domain Conformations by Ligand Binding and Cancer-Associated Mutations.Semantic proximity Read ↗

Towards In Situ Dynamics of DNA-bound Full-Length p53 TetramerSemantic proximity Read ↗

New insights into p53 function from structural studies.Semantic proximity Read ↗

Interplay of disordered and ordered regions of a human small heat shock protein yields an ensemble of “quasi-ordered” statesSemantic proximity Read ↗

Recognition of DNA by p53 core domain and location of intermolecular contacts of cooperative binding.Semantic proximity Read ↗

p53 Amino-terminus region (1-125) stabilizes and restores heat denatured p53 wild phenotype.Semantic proximity Read ↗

Crystal structure of the mouse p53 core DNA-binding domain at 2.7 A resolution.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.