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Chemical basis for the recognition of trimethyllysine by epigenetic reader proteins.


ABSTRACT: 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-? 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.

SUBMITTER: Kamps JJ 

PROVIDER: S-EPMC4673829 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature

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Chemical basis for the recognition of trimethyllysine by epigenetic reader proteins.

Kamps Jos J A G JJ   Huang Jiaxin J   Poater Jordi J   Xu Chao C   Pieters Bas J G E BJ   Dong Aiping A   Min Jinrong J   Sherman Woody W   Beuming Thijs T   Matthias Bickelhaupt F F   Li Haitao H   Mecinović Jasmin J  

Nature communications 20151118


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-π interactions  ...[more]

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