Structure of DNMT1-DNA complex reveals a role for autoinhibition in maintenance DNA methylation.

Song, Jikui; Rechkoblit, Olga; Bestor, Timothy H; Patel, Dinshaw J

Song, Jikui; Rechkoblit, Olga; Bestor, Timothy H; Patel, Dinshaw J.

Affiliation

Song J; Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA.

Science ; 331(6020): 1036-40, 2011 Feb 25.

Article in En | MEDLINE | ID: mdl-21163962

Subject(s)

DNA (Cytosine-5-)-Methyltransferases/chemistry; DNA (Cytosine-5-)-Methyltransferases/metabolism; DNA Methylation; DNA/chemistry; DNA/metabolism; Amino Acid Sequence; Animals; Catalytic Domain; Crystallography, X-Ray; Cysteine; DNA (Cytosine-5-)-Methyltransferase 1; DNA-Cytosine Methylases/chemistry; DNA-Cytosine Methylases/metabolism; Dinucleoside Phosphates/chemistry; Dinucleoside Phosphates/metabolism; Humans; Mice; Models, Molecular; Molecular Sequence Data; Mutant Proteins/chemistry; Mutant Proteins/metabolism; Nucleic Acid Conformation; Protein Binding; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Substrate Specificity

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: DNA / DNA Methylation / DNA (Cytosine-5-)-Methyltransferases Limits: Animals / Humans Language: En Journal: Science Year: 2011 Document type: Article Affiliation country: United States Country of publication: United States

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