Molecular basis of Pirh2-mediated p53 ubiquitylation

被引：0
|
作者：
Yi Sheng
Rob C Laister
Alexander Lemak
Bin Wu
Elizabeth Tai
Shili Duan
Jonathan Lukin
Maria Sunnerhagen
Sampath Srisailam
Murthy Karra
Sam Benchimol
Cheryl H Arrowsmith
机构：
[1] University of Toronto,Ontario Cancer Institute and Department of Medical Biophysics
[2] Molecular Biotechnology,Department of Biology
[3] IFM,undefined
[4] Campus Valla,undefined
[5] Linköping University,undefined
[6] York University,undefined
来源：
Nature Structural & Molecular Biology | 2008年 / 15卷
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摘要：
Pirh2 is one of several ubiquitin ligases known to modify and negatively regulate p53. Solution studies reveal the structures of the three Pirh2 domains and indicate that the C-terminal domain of Pirh2 interacts with the p53 tetramerization domain. Additional data suggest that Pirh2 preferentially modifies the tetrameric, transcriptionally active form of p53 for proteasome-mediated degradation.
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页码：1334 / 1342
页数：8
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