상세 정보

underline
Metadata Downloads : dc(xml) or Excel
Cited 0 time in scopus ci

Title 

Dual-site interactions of p53 protein transactivation domain with anti-apoptotic bcl-2 family proteins reveal a highly convergent mechanism of divergent p53 pathways

Authors 

Ji Hyang HaJ S ShinMi Kyung YoonM S LeeF HeKwang-Hee BaeH S YoonC K LeeSung Goo ParkY MutoSeung-Wook Chi

Publisher 

American Society for Biochemistry and Molecular Biology

Issue Date 

2013

Citation 

Journal of Biological Chemistry, vol. 288, no. 10, pp. 7387-7398

Keywords 

Apoptotic pathwaysAtomic levelsBcl-2 family proteinsP53 proteinStructure calculationTransactivation domain

Abstract 

Background: Interactions between p53 and Bcl-2 family proteins serve a critical role in transcription-independent p53 apoptosis. Results: We studied the interactions of p53TAD2 with anti-apoptotic Bcl-2 family proteins at the atomic level by NMR, mutagenesis, and structure calculation. Conclusion: Bcl-XL/Bcl-2, MDM2, and CBP/p300 share similar modes of binding to the dual p53TAD motifs. Significance: Dual-site interaction of p53TAD is a highly conserved mechanism in the transcription-dependent and transcription- independent p53 apoptotic pathways.

ISSN 

0021-9258

Link 

http://dx.doi.org/10.1074/jbc.M112.400754

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


There are no files associated with this item.
qrcode

FusionCharts.
DSpace Software Coptright(c) 2010 MIT and Hewleft-Packard  /  KRIBB-REPOSITORY ( Email:jakim@kribb.re.kr)