Structure of human SMYD2 protein reveals the basis of p53 tumor suppressor methylation

Journal of Biological Chemistry

Volumn 286, Issue 44, 2011, Pages 38725-38737

  Wang, Li ^a   Li, Ng ^a   Zhang, Hailong ^a   Luo, Xiao ^a   Dai, Jingquan ^a   Zhou, Shaolian ^a   Gu, Justin ^a   Zhu, Jidong ^a   Atadja, Peter ^a   Lu, Chris ^a   Li, En ^a   Zhao, Kehao ^a  

^a Novartis Institutes for Biomedical Research   (China)

Author keywords

[No Author keywords available]

Indexed keywords

BINARY COMPLEXES; C-TERMINAL DOMAINS; COFACTORS; CONFORMATIONAL CHANGE; ENZYMATIC ACTIVITIES; HIGH RESOLUTION CRYSTAL STRUCTURE; HYDROGEN BOND NETWORKS; IN-VITRO; IN-VIVO; METHYLTRANSFERASES; MOLECULAR BASIS; MONOMETHYLATION; P53 PROTEIN; S-ADENOSYLHOMOCYSTEINE; S-ADENOSYLMETHIONINE; SUBSTRATE BINDING; SUBSTRATE PEPTIDES; TERNARY COMPLEX; TERNARY STRUCTURE; TETRATRICOPEPTIDE REPEAT MOTIF; TETRATRICOPEPTIDE REPEATS; TUMOR SUPPRESSORS; U-SHAPED CONFORMATIONS;

ALKYLATION; AMINO ACIDS; HYDROGEN; HYDROGEN BONDS; METHYLATION; PEPTIDES; RUBIDIUM; TUMORS;

SUBSTRATES;

HISTONE; HISTONE LYSINE METHYLTRANSFERASE; LYSINE; PROTEIN P53; S ADENOSYLHOMOCYTEINE; S ADENOSYLMETHIONINE; SMYD2 PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; BINDING SITE; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; HUMAN; HUMAN CELL; HYDROGEN BOND; IN VITRO STUDY; IN VIVO STUDY; METHYLATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN MOTIF; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; TETRATRICOPEPTIDE REPEAT;

CALORIMETRY; CELL LINE, TUMOR; CRYSTALLOGRAPHY, X-RAY; GENES, TUMOR SUPPRESSOR; HISTONE-LYSINE N-METHYLTRANSFERASE; HISTONES; HUMANS; KINETICS; LYSINE; METHYLATION; MOLECULAR CONFORMATION; NEOPLASMS; PROTEIN BINDING; TRANSCRIPTION, GENETIC; TUMOR SUPPRESSOR PROTEIN P53;

EID: 80055096280     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.262410     Document Type: Article

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