Ontology highlight
ABSTRACT:
SUBMITTER: Otani J
PROVIDER: S-EPMC2775176 | biostudies-literature | 2009 Nov
REPOSITORIES: biostudies-literature
Otani Junji J Nankumo Toshiyuki T Arita Kyohei K Inamoto Susumu S Ariyoshi Mariko M Shirakawa Masahiro M
EMBO reports 20091016 11
DNMT3 proteins are de novo DNA methyltransferases that are responsible for the establishment of DNA methylation patterns in mammalian genomes. Here, we have determined the crystal structures of the ATRX-DNMT3-DNMT3L (ADD) domain of DNMT3A in an unliganded form and in a complex with the amino-terminal tail of histone H3. Combined with the results of biochemical analysis, the complex structure indicates that DNMT3A recognizes the unmethylated state of lysine 4 in histone H3. This finding indicates ...[more]