Crystal structures of Histone and p53 Methyltransferase SmyD2 reveal a conformational flexibility of the Autoinhibitory C-terminal domain

PLoS ONE

Volumn 6, Issue 6, 2011, Pages

  Jiang, Yuanyuan ^a   Sirinupong, Nualpun ^a   Brunzelle, Joseph ^b   Yang, Zhe ^a  

^a WAYNE STATE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b ARGONNE NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 90; HISTONE; PROTEIN METHYLTRANSFERASE; PROTEIN P53; PROTEIN SMYD1; PROTEIN SMYD2; PROTEIN SMYD3; REGULATOR PROTEIN; S ADENOSYLHOMOCYSTEINE; SINEFUNGIN; TETRATRICOPEPTIDE REPEAT PROTEIN; UNCLASSIFIED DRUG; HISTONE LYSINE METHYLTRANSFERASE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME CONFORMATION; ENZYME INHIBITION; HISTONE METHYLATION; MOUSE; NONHUMAN; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN INTERACTION; CHEMISTRY; HUMAN; METABOLISM; METHODOLOGY; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

CRYSTALLOGRAPHY, X-RAY; HISTONE-LYSINE N-METHYLTRANSFERASE; HISTONES; HUMANS; PROTEIN STRUCTURE, TERTIARY;

EID: 79959620380     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0021640     Document Type: Article

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