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Dioxygen binding in the active site of histone demethylase JMJD2A and the role of the protein environment

Abstract:

JMJD2A catalyses the demethylation of di- and trimethylated lysine residues in histone tails and is a target for the development of new anticancer medicines. Mechanistic details of demethylation are yet to be elucidated and are important for the understanding of epigenetic processes. We have evaluated the initial step of histone demethylation by JMJD2A and demonstrate the dramatic effect of the protein environment upon oxygen binding using quantum mechanics/molecular mechanics (QM/MM) calcula...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1002/chem.201502983

Authors


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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Honsby, CE More by this author
França, TC More by this author
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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
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Funding agency for:
Cortopassi, WA
Publisher:
Wiley-VCH Verlag Publisher's website
Journal:
Chemistry (Weinheim an der Bergstrasse, Germany) Journal website
Volume:
21
Issue:
52
Pages:
18983-18992
Publication date:
2015-12-05
DOI:
EISSN:
1521-3765
ISSN:
0947-6539
URN:
uuid:683bed21-4353-4156-ae03-85d4d8ad188c
Source identifiers:
589070
Local pid:
pubs:589070

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