Structure-function analysis reveals a novel mechanism for regulation of histone demethylase LSD2/AOF1/KDM1b
Zhang, Q; Qi, SK; Xu, MC; Yu, L; Tao, Y; Deng, ZQ; Wu, W; Li, JW; Chen, ZZ; Wong, JM;陶冶
刊名CELL RESEARCH
2013
卷号23期号:2页码:225-241
关键词LSD2 complex structures C4H2C2 zinc finger CW zinc finger SWIRM FAD amine oxidase
学科分类Cell Biology
DOI10.1038/cr.2012.177
英文摘要LSD2/A0F1/KDM1b catalyzes demethylation of mono- and di-methylated H3K4 and plays an important role in transcriptional regulation and genomic imprinting. Here, we report the high-resolution crystal structures of apo-LSD2 and LSD2 in complex with a peptide that mimics H3K4me2. Three structural domains of LSD2, namely, the novel N-terminal zinc finger, the centrally located SWIRM domain, and the C-terminal oxidase domain, closely pack together to form a boot-shaped structure. The active site cavity in the oxidase domain is large enough to accommodate several residues of the histone H3 tail and cannot discriminate between the different states of H3K4 methylation. The N-terminal zinc-finger domain, composed of a novel C4H2C2-type zinc finger and a specific CW-type zinc finger, is required for demethylase activity and, surprisingly, the binding of cofactor flavin adenine dinucleotide (FAD). In fact, a relay of extensive interactions through the zinc finger-SWIRM-oxidase domains is required for LSD2 demethylase activity and the binding of FAD. These results reveal a novel mechanism for the zinc finger and SWIRM domains in controlling LSD2 demethylase activity and provide a framework for elucidating the regulation and function of LSD2.
收录类别SCI
WOS记录号WOS:000315426400011
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被引频次:20[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.ihep.ac.cn/handle/311005/223898
专题中国科学院高能物理研究所_多学科研究中心_期刊论文
中国科学院高能物理研究所_多学科研究中心
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Zhang, Q,Qi, SK,Xu, MC,et al. Structure-function analysis reveals a novel mechanism for regulation of histone demethylase LSD2/AOF1/KDM1b[J]. CELL RESEARCH,2013,23(2):225-241.
APA Zhang, Q.,Qi, SK.,Xu, MC.,Yu, L.,Tao, Y.,...&Wong, JM;陶冶.(2013).Structure-function analysis reveals a novel mechanism for regulation of histone demethylase LSD2/AOF1/KDM1b.CELL RESEARCH,23(2),225-241.
MLA Zhang, Q,et al."Structure-function analysis reveals a novel mechanism for regulation of histone demethylase LSD2/AOF1/KDM1b".CELL RESEARCH 23.2(2013):225-241.
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