Ontology highlight
ABSTRACT:
SUBMITTER: Kamps JJ
PROVIDER: S-EPMC4673829 | biostudies-literature | 2015 Nov
REPOSITORIES: biostudies-literature
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]