Journal article icon

Journal article

Crystal structure of the PHF8 Jumonji domain, an Nepsilon-methyl lysine demethylase.

Abstract:

Crystallographic analysis of the catalytic domain of PHD finger protein 8 (PHF8), an N(epsilon)-methyl lysine histone demethylase associated with mental retardation and cleft lip/palate, reveals a double-stranded beta-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 fr...

Expand abstract
Publication status:
Published

Actions


Access Document


Authors


More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Role:
Author
Expand authors...
Journal:
FEBS letters
Volume:
584
Issue:
4
Pages:
825-830
Publication date:
2010-02-05
DOI:
EISSN:
1873-3468
ISSN:
0014-5793
URN:
uuid:6ce5a722-3c8a-483f-9153-239c875353fd
Source identifiers:
108265
Local pid:
pubs:108265

Terms of use


Metrics


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP