Structure-guided mutational analysis reveals the functional requirements for product specificity of DOT1 enzymes

Nature Communications

Volumn 5, Issue , 2014, Pages

  Dindar, Gülcin ^a   Anger, Andreas M ^b   Mehlhorn, Christine ^b   Hake, Sandra B ^b   Janzen, Christian J ^a  

^a UNIVERSITY OF WÜRZBURG   (Germany)

^b UNIVERSITY OF MUNICH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

DOT1 ENZYME; DOT1A ENZYME; ENZYME; HISTONE H3; UNCLASSIFIED DRUG; HISTONE LYSINE METHYLTRANSFERASE; NUCLEOSOME;

ENZYME ACTIVITY; EUKARYOTE; HOMOLOGY; MUTATION;

ARTICLE; CATALYST; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME STRUCTURE; EUKARYOTE; HYDROGEN BOND; MUTATIONAL ANALYSIS; NONHUMAN; NUCLEOSOME; SEQUENCE HOMOLOGY; TRYPANOSOMA; AMINO ACID SEQUENCE; ENZYMOLOGY; GENETICS; METABOLISM; METHYLATION; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PHYSIOLOGY; PROCEDURES; STRUCTURE ACTIVITY RELATION; TRYPANOSOMA BRUCEI BRUCEI;

EUKARYOTA;

AMINO ACID SEQUENCE; DNA MUTATIONAL ANALYSIS; HISTONE-LYSINE N-METHYLTRANSFERASE; METHYLATION; MOLECULAR SEQUENCE DATA; NUCLEOSOMES; SEQUENCE HOMOLOGY; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; TRYPANOSOMA BRUCEI BRUCEI;

EID: 84923319948     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms6313     Document Type: Article

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