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

Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations.

Science (New York, N.Y.) - 15 Jul 1994

Cho Y, Gorina S, Jeffrey P D, Pavletich N P

Abstract excerpt

Mutations in the p53 tumor suppressor are the most frequently observed genetic alterations in human cancer. The majority of the mutations occur in the core domain which contains the sequence-specific DNA binding activity of the p53 protein (residues 102-292), and they result in loss of DNA binding. The crystal structure of a complex containing the core domain of human p53 and a DNA binding site has been...

Read the complete abstract on PubMed

Topics

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

Share to DNA
Share to Genes, p53
Share to Amino Acid Sequence

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

Share to Base Sequence

Share to Binding Sites

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Conformation

Source

Identifiers

PMID: 8023157
DOI: 10.1126/science.8023157

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

Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations.PMID 8023157Read ↗

Structural biology of the tumor suppressor p53 and cancer-associated mutants.Semantic proximity Read ↗

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

Structure-function-rescue: the diverse nature of common p53 cancer mutants.Semantic proximity Read ↗

Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2.Semantic proximity Read ↗

The DNA-binding domain of p53 contains the four conserved regions and the major mutation hot spots.Semantic proximity Read ↗

Understanding the function–structure and function–mutation relationships of p53 tumor suppressor protein by high-resolution missense mutation analysisSemantic proximity Read ↗

Structural studies of p53 inactivation by DNA-contact mutations and its rescue by suppressor mutations via alternative protein-DNA interactions.Semantic proximity Read ↗

The Crystal Structure of the R280K Mutant of Human p53 Explains the Loss of DNA Binding.Semantic proximity Read ↗

Structural effects of the L145Q, V157F, and R282W cancer-associated mutations in the p53 DNA-binding core domain.Semantic proximity Read ↗

Mutational Hotspots and Conserved Domains in P53 Tumour Suppressor ProteinSemantic proximity Read ↗

Structural basis for understanding oncogenic p53 mutations and designing rescue drugsSemantic proximity Read ↗

Structural biology of the tumor suppressor p53.Semantic proximity Read ↗

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