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Structural insight into the molecular mechanism of p53-mediated mitochondrial apoptosis

Nat Commun. 2021-04; 
Hudie Wei, Lingzhi Qu, Shuyan Dai, Yun Li, Haolan Wang, Yilu Feng, Xiaojuan Chen, Longying Jiang, Ming Guo, Jun Li, Zhuchu Chen, Lin Chen, Ye Zhang, Yongheng Chen
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Proteins, Expression, Isolation and Analysis Products of the cross-linking reactions were analyzed by 4-12% SDS-PAGE (M00652, GenScript) as indicated and then silver stained Get A Quote


The tumor suppressor p53 is mutated in approximately half of all human cancers. p53 can induce apoptosis through mitochondrial membrane permeabilization by interacting with and antagonizing the anti-apoptotic proteins BCL-xL and BCL-2. However, the mechanisms by which p53 induces mitochondrial apoptosis remain elusive. Here, we report a 2.5 Å crystal structure of human p53/BCL-xL complex. In this structure, two p53 molecules interact as a homodimer, and bind one BCL-xL molecule to form a ternary complex with a 2:1 stoichiometry. Mutations at the p53 dimer interface or p53/BCL-xL interface disrupt p53/BCL-xL interaction and p53-mediated apoptosis. Overall, our current findings of the bona fide structure of p5... More