Crystal structure of the PHF8 Jumonji domain, an  N  ε ‐methyl lysine demethylase | Zendy

Yue Wyatt W. | Zendy; Hozjan Viktorija | Zendy; Ge Wei | Zendy; Loenarz Christoph | Zendy; Cooper Christopher D.O. | Zendy; Schofield Christopher J. | Zendy; Kavanagh Kathryn L. | Zendy; Oppermann Udo | Zendy; McDonough Michael A. | Zendy

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Crystal structure of the PHF8 Jumonji domain, an N ε ‐methyl lysine demethylase

Author(s) -

Yue Wyatt W.,

Hozjan Viktorija,

Ge Wei,

Loenarz Christoph,

Cooper Christopher D.O.,

Schofield Christopher J.,

Kavanagh Kathryn L.,

Oppermann Udo,

McDonough Michael A.

Publication year - 2010

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2009.12.055

Subject(s) - demethylase , phd finger , lysine , chemistry , histone , histone h3 , stereochemistry , biochemistry , helix (gastropod) , crystallography , biology , gene , amino acid , zinc finger , transcription factor , ecology , snail

Crystallographic analysis of the catalytic domain of PHD finger protein 8 (PHF8), an N ε ‐methyl lysine histone demethylase associated with mental retardation and cleft lip/palate, reveals a double‐stranded β‐helix fold with conserved Fe(II) and cosubstrate binding sites typical of the 2‐oxoglutarate dependent oxygenases. The PHF8 active site is highly conserved with those of the FBXL10/11demethylases, which are also selective for the di‐/mono‐methylated lysine states, but differs from that of the JMJD2 demethylases which are selective for tri‐/di‐methylated states. The results rationalize the lack of activity for the clinically observed F279S PHF8 variant and they will help to identify inhibitors selective for specific N ε ‐methyl lysine demethylase subfamilies.

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