Response to Comment on “Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2” | Zendy

Lianying Jiao | Zendy; Xin Liu | Zendy

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Response to Comment on “Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2”

Author(s) -

Lianying Jiao,

Xin Liu

Publication year - 2016

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.aaj2335

Subject(s) - prc2 , histone , chromatin , mutant , microbiology and biotechnology , ezh2 , histone h3 , chemistry , computational biology , biology , genetics , gene

Zhang 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.

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