Crystal structures of histone and p53 methyltransferase SmyD2 reveal a conformational flexibility of the autoinhibitory C-terminal domain

SmyD2 belongs to a new class of chromatin regulators that control gene expression in heart development and tumorigenesis. Besides methylation of histone H3 K4, SmyD2 can methylate non-histone targets including p53 and the retinoblastoma tumor suppressor. The methyltransferase activity of SmyD protei...

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Veröffentlicht in:	PloS one 2011-06, Vol.6 (6), p.e21640-e21640
Hauptverfasser:	Jiang, Yuanyuan, Sirinupong, Nualpun, Brunzelle, Joseph, Yang, Zhe
Format:	Artikel
Sprache:	eng
Schlagworte:	Automation Biochemistry Biology Cancer Catalysis Cell cycle Cell growth Chromatin Crystal structure Crystallography, X-Ray - methods Deoxyribonucleic acid Developmental biology DNA DNA methylation Epigenetics Flexibility Gene expression Genes Heat shock proteins Helices Histone H3 Histone-Lysine N-Methyltransferase - chemistry Histone-Lysine N-Methyltransferase - metabolism Histones - chemistry Histones - metabolism Hsp90 protein Humans Medicine Methylation Methyltransferase Molecular biology p53 Protein Phosphatase Protein binding Protein structure Protein Structure, Tertiary Proteins Regulators Retina Retinoblastoma Signal transduction Studies Transferases Tumor proteins Tumor suppressor genes Tumorigenesis
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