- 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...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Publisher copy:
- 10.1002/chem.201502983
-
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- 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
- Language:
- English
- Keywords:
- Copyright holder:
- Wiley-VCH Verlag GmbH and Co.
- Copyright date:
- 2015
Journal article
Dioxygen binding in the active site of histone demethylase JMJD2A and the role of the protein environment
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