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

Keyphrases

• Histone 100%
• Methyltransferase 100%
• Conformational Flexibility 100%
• SMYD2 100%
• Smyd 37%
• Tetratricopeptide Repeat 25%
• Helix 25%
• Heat Shock Protein 90 (Hsp90) 25%
• Catalytic Domain 25%
• Sinefungin 25%
• Intra-domain 25%
• Gene Expression 12%
• Tumorigenesis 12%
• Autoinhibition 12%
• Catalytic Site 12%
• Methylation 12%
• Histone H3 12%
• Control Genes 12%
• Active Sites 12%
• Conformational Change 12%
• Chromatin Regulators 12%
• Heart Development 12%
• Methyltransferase Domain 12%
• Methyltransferase Activity 12%
• Non-histone 12%
• Co-chaperone 12%
• Two-crystal 12%
• Open Form 12%
• S-adenosylhomocysteine 12%
• Structural Intermediates 12%
• Closed Conformation 12%
• Smyd1 12%
• Individual Domain 12%
• Crevice 12%
• Retinoblastoma Tumor Suppressor 12%
• SMYD3 12%
• Close-form 12%

Biochemistry, Genetics and Molecular Biology

• Crystal Structure 100%
• C-Terminus 100%
• P53 100%
• Methyltransferase 100%
• Histone 100%
• Conformation 28%
• TPR Domain 28%
• Hsp90 28%
• Enzyme Active Site 28%
• Conformational Change 14%
• Active Site 14%
• Methylation 14%
• Autoinhibition 14%
• Gene Expression Control 14%
• Tumor Suppressor Protein 14%
• Carcinogenesis 14%
• Heat Shock Protein 14%
• Histone H3 14%
• Retinoblastoma 14%
• Chlordiazepoxide 14%
• S-Adenosyl-L-Homocysteine 14%