Structure of human lysine methyltransferase Smyd2 reveals insights into the substrate divergence in Smyd proteins

Journal of Molecular Cell Biology

Volumn 3, Issue 5, 2011, Pages 293-300

  Xu, Shutong ^a,b   Zhong, Chen ^a   Zhang, Tianlong ^a   Ding, Jianping ^a  

^a INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

epigenetics; histone lysine methyltransferase; SET family; Smyd proteins; Smyd2

Indexed keywords

DNA BINDING PROTEIN; HISTONE; HISTONE LYSINE METHYLTRANSFERASE; ISOENZYME; LYSINE; MUSCLE PROTEIN; PROTEIN P53; S ADENOSYLHOMOCYSTEINE; SMYD1 PROTEIN, HUMAN; SMYD2 PROTEIN, HUMAN; SMYD3 PROTEIN, HUMAN; TRANSCRIPTION FACTOR;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME SPECIFICITY; HUMAN; METABOLISM; MOLECULAR GENETICS; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DNA-BINDING PROTEINS; HISTONE-LYSINE N-METHYLTRANSFERASE; HISTONES; HUMANS; ISOENZYMES; LYSINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUSCLE PROTEINS; PROTEIN STRUCTURE, TERTIARY; S-ADENOSYLHOMOCYSTEINE; SUBSTRATE SPECIFICITY; TRANSCRIPTION FACTORS; TUMOR SUPPRESSOR PROTEIN P53;

EID: 80455176677     PISSN: 16742788     EISSN: 17594685     Source Type: Journal    
DOI: 10.1093/jmcb/mjr015     Document Type: Article

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