Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor

被引:125
|
作者
Pascual, J
Martinez-Yamout, M
Dyson, HJ
Wright, PE
机构
[1] Scripps Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA
[2] Scripps Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA
基金
美国国家卫生研究院;
关键词
transcriptional regulation; NMR structure; gene silencing;
D O I
10.1006/jmbi.2000.4308
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The PHD (plant homeo domain) is a similar to 50-residue motif found mainly in proteins involved in eukaryotic transcription regulation. The characteristic sequence feature is a conserved Cys(4)-HisCys(3) zinc binding motif. We have determined the solution structure of the PHD motif from the human Williams-Beuren syndrome transcription factor (WSTF) protein. The domain folds into an interleaved zinc finger which binds two Zn2+ in a similar manner to that of the RING and FYVE domains. The structure reveals a conserved zinc-binding core, together with two variable loops that are likely candidates for interactions between the various PHD domains and their specific ligands. (C) 2000 Academic Press.
引用
收藏
页码:723 / 729
页数:7
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