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

Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2.

Science (New York, N.Y.) - 16 Oct 2015

Jiao Lianying, Liu Xin

Abstract excerpt

Polycomb repressive complex 2 (PRC2) catalyzes histone H3K27 trimethylation (H3K27me3), a hallmark of gene silencing. Here we report the crystal structures of an active PRC2 complex of 170 kilodaltons from the yeast Chaetomium thermophilum in both basal and stimulated states, which contain Ezh2, Eed, and the VEFS domain of Suz12 and are bound to a cancer-associated inhibiting H3K27M peptide and a...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Catalysis
Share to Catalytic Domain

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

Share to Gene Silencing

Share to Histones

Share to Jumonji Domain-Containing Histone Demethylases

Share to Methylation

Share to Polycomb Repressive Complex 2

Source

Open in PubMed Open full text

Identifiers

PMID: 26472914
DOI: 10.1126/science.aac4383
PMCID: PMC5220110

Genes

SET

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

Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2.PMID 26472914Read ↗

Polycomb repressive complex 2 in an autoinhibited state.Semantic proximity Read ↗

Structure of the catalytic domain of EZH2 reveals conformational plasticity in cofactor and substrate binding sites and explains oncogenic mutations.Semantic proximity Read ↗

Structural context of disease-associated mutations and putative mechanism of autoinhibition revealed by X-ray crystallographic analysis of the EZH2-SET domain.Semantic proximity Read ↗

Structural basis for PRC2 decoding of active histone methylation marks H3K36me2/3.Semantic proximity Read ↗

The conserved N-terminal SANT1-binding domain (SBD) of EZH2 regulates PRC2 activity.Semantic proximity Read ↗

The conserved N-terminal SANT1-binding domain (SBD) of EZH2 Regulates PRC2 ActivitySemantic proximity Read ↗

Structural basis of oncogenic histone H3K27M inhibition of human polycomb repressive complex 2.Semantic proximity Read ↗

Structure of the PRC2 complex and application to drug discovery.Semantic proximity Read ↗

Histone methylation by PRC2 is inhibited by active chromatin marks.Semantic proximity Read ↗

Regulation of histone methylation by automethylation of PRC2Semantic proximity Read ↗

Visualization of PRC2-Dinucleosome Interactions Leading to Epigenetic RepressionSemantic proximity Read ↗

<i>Caenorhabditis elegans</i> MES-3 is a highly divergent ortholog of the canonical PRC2 component SUZ12Semantic proximity Read ↗

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