Structure of Dnmt3a bound to Dnmt3L suggests a model for de novo DNA methylation
Da Jia,
Renata Z. Jurkowska,
Xing Zhang,
Albert Jeltsch () and
Xiaodong Cheng ()
Additional contact information
Da Jia: Emory University School of Medicine, 1510 Clifton Road, Atlanta, Georgia 30322, USA
Renata Z. Jurkowska: Biochemistry Laboratory, School of Engineering and Science, Jacobs University Bremen, Campus Ring 1
Xing Zhang: Emory University School of Medicine, 1510 Clifton Road, Atlanta, Georgia 30322, USA
Albert Jeltsch: Biochemistry Laboratory, School of Engineering and Science, Jacobs University Bremen, Campus Ring 1
Xiaodong Cheng: Emory University School of Medicine, 1510 Clifton Road, Atlanta, Georgia 30322, USA
Nature, 2007, vol. 449, issue 7159, 248-251
Abstract:
A crystal structure of a complex between the DNA methyltransferase regulatory factor Dnmt3L and the catalytic domain of Dnmt3a leads to a model being proposed for the preferential methylation of DNA on maternally imprinted genes.
Date: 2007
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DOI: 10.1038/nature06146
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