Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet

EMBO Journal

Volumn 22, Issue 2, 2003, Pages 292-303

  Kwon, Taewoo ^a   Chang, Jeong Ho ^a   Kwak, Eunyee ^a   Lee, Chang Wook ^a   Joachimiak, Andrzej ^b   Kim, Young Chang ^b   Lee, Jae Woon ^a   Cho, Yunje ^a  

^a Pohang University of Science and Technology (POSTECH)   (South Korea)

^b ARGONNE NATIONAL LABORATORY   (United States)

Author keywords

9 histone methyltransferase; Compact form of AdoMet; Post SET helix; SET domain; SET7; Substrate specific channel

Indexed keywords

HISTONE; HISTONE LYSINE METHYLTRANSFERASE; PROTEIN SET7 9; UNCLASSIFIED DRUG;

ARTICLE; CHROMATIN STRUCTURE; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; GENE EXPRESSION REGULATION; METHYLATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; HISTONE-LYSINE N-METHYLTRANSFERASE; HISTONES; HUMANS; LYSINE; METHYLATION; METHYLTRANSFERASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; REPRESSOR PROTEINS; S-ADENOSYLMETHIONINE; SEQUENCE ALIGNMENT;

EID: 0037439085     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdg025     Document Type: Article

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