Structural insights into a dual-specificity histone demethylase ceKDM7A from Caenorhabditis elegans

Histone lysine methylation can be removed by JmjC domain-containing proteins in a sequence- and methylationstate-specific manner. However, how substrate specificity is determined and how the enzymes are regulated were largely unknown. We recently found that ceKDM7A, a PHD- and JmjC domain-containing...

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Veröffentlicht in:	Cell research 2010-08, Vol.20 (8), p.886-898
Hauptverfasser:	Yang, Ying, Hu, Lulu, Wang, Ping, Hou, Haifeng, Lin, Yan, Liu, Yi, Li, Ze, Gong, Rui, Feng, Xiang, Zhou, Lu, Zhang, Wen, Dong, Yuhui, Yang, Huirong, Lin, Hanqing, Wang, Yiqin, Chen, Charlie Degui, Xu, Yanhui
Format:	Artikel
Sprache:	eng
Schlagworte:	631/45/535 Amino Acid Substitution Animals Biomedical and Life Sciences Caenorhabditis elegans - enzymology Caenorhabditis elegans Proteins - chemistry Caenorhabditis elegans Proteins - metabolism Catalytic Domain Cell Biology Computer Simulation Crystallography, X-Ray Enzymatic activity Histones - metabolism Jumonji Domain-Containing Histone Demethylases - chemistry Jumonji Domain-Containing Histone Demethylases - metabolism Life Sciences Methylation Molecular Sequence Data original-article Peptides Protein Binding Protein Structure, Tertiary Sequence Alignment Sequence Homology, Amino Acid Substrate Specificity Substrates 催化结构域分子机制底物特异性晶体结构甲基化酶组蛋白脱甲基
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