Polycomb repressive complex 2 in an autoinhibited state
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Summary
The crystal structure of an apo-PRC2 from the fungus Chaetomium thermophilum captured in a bona fide autoinhibited state is determined, which represents a novel conformation of PRC2 associated with enzyme regulation in light of the basal and stimulated states that were reported previously.
- Type
- article
- Published
- 2017-06-12
- Cited by
- 16
- References
- 34
- Access
- Open access
- OpenAlex
- https://openalex.org/W2625852109
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:22348327
Keywords
PRC2, Histone H3, Polycomb-group proteins, Biology, Chromatin
References
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Cited by
- Structure, mechanism, and regulation of polycomb-repressive complex 2
- Towards the structural characterization of the human methyltransferome.
- An Evolutionarily Conserved Structural Platform for PRC2 Inhibition by a Class of Ezh2 Inhibitors
- Recent structural insights into PRC2 regulation and substrate binding
- Automethylation of PRC2 promotes H3K27 methylation and is impaired in H3K27M pediatric glioma
- Engaging chromatin: PRC2 structure meets function
- A Structural Perspective on Gene Repression by Polycomb Repressive Complex 2.
- Polycomb gene silencing mechanisms: PRC2 chromatin targeting, H3K27me3 “readout” and phase separation-based compaction
- Allosteric regulation of histone lysine methyltransferases: from context-specific regulation to selective drugs
- Activation of Histone 3 Lysine 9 methyl writing and reading capabilities within the G9a-GLP heterodimer
- Heterodimerization of H3K9 histone methyltransferases G9a and GLP activates methyl reading and writing capabilities
- Recent strategies targeting Embryonic Ectoderm Development (EED) for cancer therapy: Allosteric inhibitors, PPI inhibitors, and PROTACs.
- Polycomb Repressive Complex 2 in Eukaryotes—An Evolutionary Perspective
- Macromolecular Protein Complexes III: Structure and Function
- Epigenetic regulation of embryonic ectoderm development in stem cell differentiation and transformation during ontogenesis
- The N-terminal methyltransferase homologs NRMT1 and NRMT2 exhibit novel regulation of activity through heterotrimer formation.
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