The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules

Nature Structural and Molecular Biology

Volumn 15, Issue 3, 2008, Pages 245-250

  Collins, Robert E ^a   Northrop, Jeffrey P ^b   Horton, John R ^a   Lee, David Y ^b   Zhang, Xing ^a   Stallcup, Michael R ^b   Cheng, Xiaodong ^a  

^a EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; HISTONE METHYLTRANSFERASE; LYSINE; TRYPTOPHAN; EUCHROMATIC HISTONE METHYLTRANSFERASE 1; G9A HISTONE METHYLTRANSFERASE, MOUSE; HISTONE; HISTONE LYSINE METHYLTRANSFERASE; METHYLTRANSFERASE; MUTANT PROTEIN; PEPTIDE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; HUMAN; HYDROPHOBICITY; METHYLATION; MOUSE; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE; X RAY CRYSTALLOGRAPHY; ANIMAL; CELL STRAIN COS1; CERCOPITHECUS; CHEMISTRY; GENETICS; METABOLISM; MUTATION;

ANIMALS; ANKYRIN REPEAT; CERCOPITHECUS AETHIOPS; COS CELLS; HISTONE-LYSINE N-METHYLTRANSFERASE; HISTONES; HUMANS; LYSINE; METHYLATION; METHYLTRANSFERASES; MICE; MUTANT PROTEINS; MUTATION; PEPTIDES; PROTEIN BINDING;

EID: 40949148102     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1384     Document Type: Article

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