The DNA-binding domain mediates both nuclear and cytosolic functions of p53

被引：0
作者：
Ariele Viacava Follis
Fabien Llambi
Li Ou
Katherine Baran
Douglas R Green
Richard W Kriwacki
机构：
[1] St. Jude Children's Research Hospital,Department of Structural Biology
[2] St. Jude Children's Research Hospital,Department of Immunology
[3] Immunology and Biochemistry,Department of Microbiology
[4] University of Tennessee Health Sciences Center,undefined
来源：
Nature Structural & Molecular Biology | 2014年 / 21卷
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摘要：
Tumor suppressor p53 can activate BAX or BAK; this activity is opposed by antiapoptotic protein BCL-xL, which sequesters p53. Now Kriwacki, Green and colleagues characterize the human p53–BCL-xL complex by NMR spectroscopy, thus allowing mutagenesis analyses to dissect p53's nuclear and cytosolic functions and BCL-xL's antiapoptotic mechanisms.
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页码：535 / 543
页数：8
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