Journal
NATURE COMMUNICATIONS
Volume 6, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms9911
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Funding
- Netherlands Research School for Chemical Biology
- National Natural Science Foundation of China program [31270763]
- Major State Basic Research Development Program in China [2015CB910503]
- Netherlands Organization for Scientific Research (NWO-ALW)
- AbbVie
- Boehringer Ingelheim
- Canada Foundation for Innovation
- Genome Canada through the Ontario Genomics Institute [OGI-055]
- GlaxoSmithKline
- Janssen
- Lilly Canada
- Novartis Research Foundation
- Ontario Ministry of Economic Development and Innovation
- Pfizer
- Takeda
- Wellcome Trust [092809/Z/10/Z]
- Netherlands Organization for Scientific Research (NWO-CW)
- Netherlands Organization for Scientific Research (NWO-EW)
- Canadian Institutes for Health Research,
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A large number of structurally diverse epigenetic reader proteins specifically recognize methylated lysine residues on histone proteins. Here we describe comparative thermodynamic, structural and computational studies on recognition of the positively charged natural trimethyllysine and its neutral analogues by reader proteins. This work provides experimental and theoretical evidence that reader proteins predominantly recognize trimethyllysine via a combination of favourable cation-pi interactions and the release of the high-energy water molecules that occupy the aromatic cage of reader proteins on the association with the trimethyllysine side chain. These results have implications in rational drug design by specifically targeting the aromatic cage of readers of trimethyllysine.
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