5kjh
Crystal structure of an active polycomb repressive complex 2 in the stimulated state
Structural highlights
FunctionEED_CHATD Component of the of the Polycomb Repressive Complex 2 (PRC2), a histone H3 lysine methyltransferase responsible for generating mono-, di-, and tri-methylation on Lys27 (H3K27me1, H3K27me2 and H3K27me3) (PubMed:26472914, PubMed:29904056). The tri-methylated form is known to be critical in gene repression, and its proper placement is essential in defining repression patterns during development (PubMed:26472914, PubMed:28008037, PubMed:28607149, PubMed:29904056). EED is not a catalytic subunit but is required for the complex regulation of histone H3 lysine methylation by EZH2 (PubMed:26472914, PubMed:28008037, PubMed:28607149, PubMed:29904056).[1] [2] [3] [4] Publication Abstract from PubMedZhang et al suggested that in the crystal structure of a polycomb repressive complex 2 from Chaetomium thermophilum (ctPRC2), a flexible linker region, but not the H3K27M cancer mutant peptide, better fits the electron density. Based on our new data, we agree with this alternative interpretation and provide the crystal structure of ctPRC2 bound to a bona fide H3K27M sequence. Response to Comment on "Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2".,Jiao L, Liu X Science. 2016 Dec 23;354(6319):1543. doi: 10.1126/science.aaj2335. PMID:28008038[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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