title: Comment on "Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2".
abstract: Jiao and Liu (Research Articles, 16 October 2015, aac4383) reported the crystal structure of the protein complex polycomb repressive complex 2 from Chaetomium thermophilum This landmark structure has brought invaluable insights into the activation mechanism of this essential methyltransferase. However, the analysis of the x-ray data discussed below suggests that the description of oncogenic H3K27M peptide binding to the active site is incorrect.
authors.affiliation: Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
authors.forename: Ying
authors.initials: Y
authors.lastname: Zhang
authors.affiliation: Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
authors.forename: Neil
authors.initials: N
authors.lastname: Justin
authors.affiliation: Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
authors.forename: Jon R
authors.initials: JR
authors.lastname: Wilson
authors.affiliation: Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK. steve.gamblin@crick.ac.uk.
authors.forename: Steven J
authors.initials: SJ
authors.lastname: Gamblin
mesh_terms: D002597:Chaetomium / Q000378:metabolism; D006657:Histones / Q000378:metabolism*; D008745:Methylation; D063150:Polycomb Repressive Complex 1 / Q000378:metabolism; D063151:Polycomb Repressive Complex 2 / Q000737:chemistry*
chemical_list: D006657:Histones; D063151:Polycomb Repressive Complex 2; D063150:Polycomb Repressive Complex 1